1M9C

X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) M-type Complex.

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations
Structure Motif: Primary M-CSA Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1m9ca_	All beta proteins	Cyclophilin-like	Cyclophilin-like	Cyclophilin (peptidylprolyl isomerase)	Cyclophilin (eukaryotic)	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d1m9cb_	All beta proteins	Cyclophilin-like	Cyclophilin-like	Cyclophilin (peptidylprolyl isomerase)	Cyclophilin (eukaryotic)	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d1m9cc_	All alpha proteins	Retrovirus capsid protein, N-terminal core domain	Retrovirus capsid protein, N-terminal core domain	Retrovirus capsid protein, N-terminal core domain	HIV-1 capsid protein	(Human immunodeficiency virus 1 ) [TaxId: 11676 ],	SCOPe (2.08)
D	d1m9cd_	All alpha proteins	Retrovirus capsid protein, N-terminal core domain	Retrovirus capsid protein, N-terminal core domain	Retrovirus capsid protein, N-terminal core domain	HIV-1 capsid protein	(Human immunodeficiency virus 1 ) [TaxId: 11676 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Cyclophilin-like	8043341	3000168	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Cyclophilin-like	8043341	3000168	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF00160	e1m9cA1	A: beta barrels	X: Cyclophilin-like (From Topology)	H: Cyclophilin-like (From Topology)	T: Cyclophilin-like	F: PF00160	ECOD (1.6)
B	PF00160	e1m9cB1	A: beta barrels	X: Cyclophilin-like (From Topology)	H: Cyclophilin-like (From Topology)	T: Cyclophilin-like	F: PF00160	ECOD (1.6)
C	PF00607	e1m9cC1	A: alpha bundles	X: Retrovirus capsid protein	H: Retrovirus capsid protein N-terminal domain (From Topology)	T: Retrovirus capsid protein N-terminal domain	F: PF00607	ECOD (1.6)
D	PF00607	e1m9cD1	A: alpha bundles	X: Retrovirus capsid protein	H: Retrovirus capsid protein N-terminal domain (From Topology)	T: Retrovirus capsid protein N-terminal domain	F: PF00607	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.40.100.10	Mainly Beta	Beta Barrel	Cyclophilin	Cyclophilin-like	CATH (4.3.0)
B	2.40.100.10	Mainly Beta	Beta Barrel	Cyclophilin	Cyclophilin-like	CATH (4.3.0)
C	1.10.375.10	Mainly Alpha	Orthogonal Bundle	Human Immunodeficiency Virus Type 1 Capsid Protein	Human Immunodeficiency Virus Type 1 Capsid Protein	CATH (4.3.0)
D	1.10.375.10	Mainly Alpha	Orthogonal Bundle	Human Immunodeficiency Virus Type 1 Capsid Protein	Human Immunodeficiency Virus Type 1 Capsid Protein	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00160	Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD (Pro_isomerase)	Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD	The peptidyl-prolyl cis-trans isomerases, also known as cyclophilins, share this domain of about 109 amino acids. Cyclophilins have been found in all organisms studied so far and catalyse peptidyl-prolyl isomerisation during which the peptide bond pr ...	The peptidyl-prolyl cis-trans isomerases, also known as cyclophilins, share this domain of about 109 amino acids. Cyclophilins have been found in all organisms studied so far and catalyse peptidyl-prolyl isomerisation during which the peptide bond preceding proline (the peptidyl-prolyl bond) is stabilised in the cis conformation. Mammalian cyclophilin A (CypA) is a major cellular target for the immunosuppressive drug cyclosporin A (CsA). Other roles for cyclophilins may include chaperone and cell signalling function [1].	Domain
C, D	PF00607	gag protein p24 N-terminal domain (Gag_p24)	gag protein p24 N-terminal domain	p24 forms inner protein layer of the nucleocapsid. ELISA tests for p24 is the most commonly used method to demonstrate virus replication both in vivo and in vitro.	Domain
C, D	PF19317	Gag protein p24 C-terminal domain (Gag_p24_C)	Gag protein p24 C-terminal domain	p24 forms inner protein layer of the nucleocapsid. ELISA tests for p24 is the most commonly used method to demonstrate virus replication both in vivo and in vitro.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Cyclophilin A	amide binding binding cyclosporin A binding isomerase activity catalytic activity, acting on a protein peptidyl-prolyl cis-trans isomerase activity catalytic activity cis-trans isomerase activity glycosaminoglycan binding organic acid binding ion binding heparan sulfate binding anion binding carboxylic acid binding amide binding binding cyclosporin A binding isomerase activity catalytic activity, acting on a protein peptidyl-prolyl cis-trans isomerase activity catalytic activity cis-trans isomerase activity glycosaminoglycan binding organic acid binding ion binding heparan sulfate binding anion binding carboxylic acid binding carbohydrate derivative binding small molecule binding sulfur compound binding RNA binding organic cyclic compound binding nucleic acid binding cell adhesion molecule binding protein-containing complex binding protein binding integrin binding signaling receptor binding unfolded protein binding virion binding	cellular response to stimulus regulation of cellular process response to stimulus signaling negative regulation of signaling negative regulation of intracellular signal transduction negative regulation of stress-activated MAPK cascade negative regulation of biological process regulation of cellular response to stress regulation of signal transduction intracellular signal transduction negative regulation of cell communication cell communication stress-activated MAPK cascade cellular response to stress cellular response to stimulus regulation of cellular process response to stimulus signaling negative regulation of signaling negative regulation of intracellular signal transduction negative regulation of stress-activated MAPK cascade negative regulation of biological process regulation of cellular response to stress regulation of signal transduction intracellular signal transduction negative regulation of cell communication cell communication stress-activated MAPK cascade cellular response to stress regulation of intracellular signal transduction response to stress regulation of response to stress intracellular signaling cassette negative regulation of cellular process signal transduction regulation of biological process regulation of signaling negative regulation of response to stimulus biological regulation regulation of stress-activated protein kinase signaling cascade regulation of MAPK cascade negative regulation of signal transduction regulation of stress-activated MAPK cascade stress-activated protein kinase signaling cascade regulation of response to stimulus negative regulation of stress-activated protein kinase signaling cascade MAPK cascade regulation of cell communication cellular process negative regulation of MAPK cascade regulation of apoptotic process regulation of programmed cell death cell death apoptotic signaling pathway apoptotic process programmed cell death regulation of apoptotic signaling pathway organonitrogen compound metabolic process cellular biosynthetic process cellular metabolic process primary metabolic process gene expression macromolecule biosynthetic process protein maturation organic substance metabolic process protein folding biosynthetic process organic substance biosynthetic process metabolic process protein metabolic process macromolecule metabolic process positive regulation of phosphorylation regulation of catalytic activity regulation of transferase activity positive regulation of phosphate metabolic process regulation of primary metabolic process positive regulation of metabolic process regulation of phosphate metabolic process phosphate-containing compound metabolic process positive regulation of macromolecule metabolic process phosphorus metabolic process protein modification process positive regulation of protein phosphorylation protein phosphorylation positive regulation of phosphorus metabolic process phosphorylation regulation of protein metabolic process regulation of cellular metabolic process regulation of molecular function positive regulation of kinase activity regulation of kinase activity activation of protein kinase activity macromolecule modification regulation of phosphorus metabolic process regulation of metabolic process regulation of protein modification process regulation of protein phosphorylation positive regulation of protein metabolic process positive regulation of biological process positive regulation of cellular metabolic process positive regulation of molecular function positive regulation of protein modification process activation of protein kinase B activity positive regulation of protein kinase activity positive regulation of cellular process positive regulation of transferase activity positive regulation of catalytic activity regulation of protein kinase activity regulation of macromolecule metabolic process regulation of phosphorylation cell chemotaxis chemotaxis neutrophil chemotaxis response to external stimulus neutrophil migration granulocyte migration leukocyte migration cellular response to chemical stimulus taxis immune system process granulocyte chemotaxis response to chemical myeloid leukocyte migration cell migration cell motility leukocyte chemotaxis locomotion negative regulation of phosphate metabolic process negative regulation of cellular metabolic process negative regulation of protein modification process negative regulation of protein metabolic process negative regulation of macromolecule metabolic process negative regulation of metabolic process negative regulation of protein phosphorylation negative regulation of phosphorus metabolic process negative regulation of phosphorylation multicellular organismal process regulation of body fluid levels wound healing homotypic cell-cell adhesion cell activation hemostasis platelet aggregation blood coagulation cell adhesion cell-cell adhesion coagulation regulation of biological quality response to wounding platelet activation response to oxidative stress cellular response to oxidative stress cellular response to chemical stress negative regulation of catalytic activity negative regulation of kinase activity negative regulation of transferase activity negative regulation of molecular function negative regulation of protein kinase activity negative regulation of viral process regulation of viral process regulation of viral life cycle negative regulation of viral life cycle viral process viral life cycle positive regulation of DNA-binding transcription factor activity positive regulation of NF-kappaB transcription factor activity RNA metabolic process nucleobase-containing compound metabolic process RNA biosynthetic process nucleic acid biosynthetic process DNA-templated transcription regulation of RNA metabolic process regulation of nucleobase-containing compound metabolic process regulation of RNA biosynthetic process regulation of biosynthetic process nucleobase-containing compound biosynthetic process nucleic acid metabolic process regulation of cellular biosynthetic process organic cyclic compound metabolic process regulation of gene expression regulation of DNA-binding transcription factor activity organic cyclic compound biosynthetic process regulation of macromolecule biosynthetic process regulation of DNA-templated transcription cellular component organization organelle organization lipid droplet organization cellular component organization or biogenesis positive regulation of viral genome replication positive regulation of viral process viral genome replication regulation of viral genome replication peptidyl-amino acid modification peptidyl-proline modification protein peptidyl-prolyl isomerization developmental process cellular developmental process nervous system development generation of neurons neurogenesis multicellular organism development neuron differentiation cell differentiation anatomical structure development system development negative regulation of post-translational protein modification regulation of protein K48-linked ubiquitination regulation of protein ubiquitination protein ubiquitination regulation of protein modification by small protein conjugation or removal negative regulation of protein ubiquitination regulation of protein polyubiquitination negative regulation of protein modification by small protein conjugation or removal regulation of post-translational protein modification protein polyubiquitination negative regulation of protein K48-linked ubiquitination negative regulation of protein polyubiquitination post-translational protein modification protein K48-linked ubiquitination protein modification by small protein conjugation protein modification by small protein conjugation or removal positive regulation of cell communication positive regulation of signal transduction positive regulation of response to stimulus positive regulation of MAPK cascade positive regulation of intracellular signal transduction positive regulation of signaling protein localization regulation of localization establishment of protein localization cellular localization nitrogen compound transport regulation of protein localization transport positive regulation of establishment of protein localization positive regulation of secretion by cell protein localization to extracellular region positive regulation of protein transport localization regulation of secretion by cell secretion by cell positive regulation of secretion cellular macromolecule localization regulation of transport secretion organic substance transport regulation of establishment of protein localization establishment of protein localization to extracellular region export from cell regulation of protein transport protein secretion establishment of localization positive regulation of protein secretion regulation of protein secretion regulation of secretion positive regulation of transport protein transport regulation of cellular localization macromolecule localization positive regulation of protein localization intrinsic apoptotic signaling pathway in response to oxidative stress regulation of oxidative stress-induced intrinsic apoptotic signaling pathway regulation of intrinsic apoptotic signaling pathway negative regulation of apoptotic signaling pathway intrinsic apoptotic signaling pathway negative regulation of programmed cell death negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway negative regulation of intrinsic apoptotic signaling pathway negative regulation of apoptotic process exit from host cell biological process involved in interspecies interaction between organisms viral release from host cell biological process involved in interaction with host biological process involved in symbiotic interaction cell adhesion molecule production protein dephosphorylation positive regulation of dephosphorylation regulation of dephosphorylation regulation of protein dephosphorylation dephosphorylation positive regulation of protein dephosphorylation endothelial cell activation	membrane cellular anatomical entity extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol membrane cellular anatomical entity extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol anchoring junction cell junction focal adhesion cell-substrate junction membrane-enclosed lumen intracellular vesicle ficolin-1-rich granule intracellular membrane-bounded organelle endomembrane system intracellular organelle lumen intracellular organelle organelle lumen cytoplasmic vesicle ficolin-1-rich granule lumen secretory granule secretory vesicle protein-containing complex vesicle lumen cytoplasmic vesicle lumen secretory granule lumen nucleus
C, D	HIV-1 Capsid	structural molecule activity cation binding transition metal ion binding zinc ion binding ion binding binding metal ion binding small molecule binding RNA binding organic cyclic compound binding nucleic acid binding	virion assembly viral process viral budding viral budding via host ESCRT complex viral life cycle	virion component virion membrane viral nucleocapsid viral capsid intracellular anatomical structure cytoplasm cellular anatomical entity host cellular component host intracellular part host cell cytoplasm host cell part host intracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR029000	Cyclophilin-like domain superfamily	Homologous Superfamily
A, B	IPR002130	Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain	Domain
A, B	IPR024936	Cyclophilin-type peptidyl-prolyl cis-trans isomerase	Family
A, B	IPR020892	Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved site	Conserved Site
C, D	IPR000071	Immunodeficiency lentiviral matrix, N-terminal	Domain
C, D	IPR045345	Retroviral nucleocapsid Gag protein p24, C-terminal domain	Domain
C, D	IPR036875	Zinc finger, CCHC-type superfamily	Homologous Superfamily
C, D	IPR001878	Zinc finger, CCHC-type	Domain
C, D	IPR008919	Retrovirus capsid, N-terminal	Homologous Superfamily
C, D	IPR010999	Retroviral matrix protein	Homologous Superfamily
C, D	IPR012344	Matrix protein, lentiviral and alpha-retroviral, N-terminal	Homologous Superfamily
C, D	IPR014817	Gag protein p6	Domain
C, D	IPR008916	Retrovirus capsid, C-terminal	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B	Pharos: P62937	squamous cell carcinoma non-small cell lung carcinoma Neoplasm Metastasis rheumatoid arthritis breast cancer gastric neoplasm mucocutaneous lymph node syndrome ovarian cancer peripheral nervous system disease schizophrenia dry eye syndrome hereditary diffuse gastric adenocarcinoma myopathy oral cavity neoplasm pancreatic intraductal papillary-mucinous carcinoma squamous cell carcinoma non-small cell lung carcinoma Neoplasm Metastasis rheumatoid arthritis breast cancer gastric neoplasm mucocutaneous lymph node syndrome ovarian cancer peripheral nervous system disease schizophrenia dry eye syndrome hereditary diffuse gastric adenocarcinoma myopathy oral cavity neoplasm pancreatic intraductal papillary-mucinous carcinoma peripheral neuropathy gastric cancer juvenile dermatomyositis osteosarcoma pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	peptidylprolyl isomerase (cyclophilin-type) M-CSA #189	The cyclophilin family of enzymes catalyses the cis-trans isomerisation of peptide bonds preceding proline residues. This activity accelerates protein folding in vitro and may underlie some of the many roles of cyclophilins, which include signalling, mitochondrial function, chaperone activity, RNA splicing, stress response, gene expression and regulation of kinase activity. The biological activities of cyclophilin A (CypA) in humans include binding the HIV-1 CA protein in the virions and facilitating viral replication; the basis for this is unclear and isomerase activity is not required for HIV-1 infectivity.	Defined by 7 residues: ARG:A-55PHE:A-60GLN:A-63ASN:A-102PHE:A-113LEU:A-122HIS:A-126 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 5.2.1.8 (PDB Primary Data) Search M-CSA Motif + EC 5.2.1.8

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.