3CIA

Crystal structure of cold-aminopeptidase from Colwellia psychrerythraea

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
C	PF17900	e3ciaC2	A: beta sandwiches	X: Baculovirus p35 protein-related (From Topology)	H: Baculovirus p35 protein-related (From Topology)	T: Baculovirus p35 protein-related	F: PF17900	ECOD (1.6)
C	PF09127	e3ciaC3	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: PF09127	ECOD (1.6)
C	PF01433	e3ciaC1	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: PF01433	ECOD (1.6)
D	PF17900	e3ciaD2	A: beta sandwiches	X: Baculovirus p35 protein-related (From Topology)	H: Baculovirus p35 protein-related (From Topology)	T: Baculovirus p35 protein-related	F: PF17900	ECOD (1.6)
D	PF09127	e3ciaD3	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: PF09127	ECOD (1.6)
D	PF01433	e3ciaD1	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: PF01433	ECOD (1.6)
A	PF17900	e3ciaA2	A: beta sandwiches	X: Baculovirus p35 protein-related (From Topology)	H: Baculovirus p35 protein-related (From Topology)	T: Baculovirus p35 protein-related	F: PF17900	ECOD (1.6)
A	PF09127	e3ciaA3	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: PF09127	ECOD (1.6)
A	PF01433	e3ciaA1	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: PF01433	ECOD (1.6)
B	PF17900	e3ciaB2	A: beta sandwiches	X: Baculovirus p35 protein-related (From Topology)	H: Baculovirus p35 protein-related (From Topology)	T: Baculovirus p35 protein-related	F: PF17900	ECOD (1.6)
B	PF09127	e3ciaB3	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: PF09127	ECOD (1.6)
B	PF01433	e3ciaB1	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: PF01433	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
C	2.60.40.1730	Mainly Beta	Sandwich	Immunoglobulin-like	tricorn interacting facor f3 domain	CATH (4.3.0)
C	3.30.2010.30	Alpha Beta	2-Layer Sandwich	Zincin-like		CATH (4.3.0)
C	1.10.390.10	Mainly Alpha	Orthogonal Bundle	Neutral Protease	domain 2	CATH (4.3.0)
C	1.25.40.320	Mainly Alpha	Alpha Horseshoe	Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat	Peptidase M1, leukotriene A4 hydrolase/aminopeptidase C-terminal domain	CATH (4.3.0)
D	2.60.40.1730	Mainly Beta	Sandwich	Immunoglobulin-like	tricorn interacting facor f3 domain	CATH (4.3.0)
D	3.30.2010.30	Alpha Beta	2-Layer Sandwich	Zincin-like		CATH (4.3.0)
D	1.10.390.10	Mainly Alpha	Orthogonal Bundle	Neutral Protease	domain 2	CATH (4.3.0)
D	1.25.40.320	Mainly Alpha	Alpha Horseshoe	Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat	Peptidase M1, leukotriene A4 hydrolase/aminopeptidase C-terminal domain	CATH (4.3.0)
A	2.60.40.1730	Mainly Beta	Sandwich	Immunoglobulin-like	tricorn interacting facor f3 domain	CATH (4.3.0)
A	3.30.2010.30	Alpha Beta	2-Layer Sandwich	Zincin-like		CATH (4.3.0)
A	1.10.390.10	Mainly Alpha	Orthogonal Bundle	Neutral Protease	domain 2	CATH (4.3.0)
A	1.25.40.320	Mainly Alpha	Alpha Horseshoe	Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat	Peptidase M1, leukotriene A4 hydrolase/aminopeptidase C-terminal domain	CATH (4.3.0)
B	2.60.40.1730	Mainly Beta	Sandwich	Immunoglobulin-like	tricorn interacting facor f3 domain	CATH (4.3.0)
B	3.30.2010.30	Alpha Beta	2-Layer Sandwich	Zincin-like		CATH (4.3.0)
B	1.10.390.10	Mainly Alpha	Orthogonal Bundle	Neutral Protease	domain 2	CATH (4.3.0)
B	1.25.40.320	Mainly Alpha	Alpha Horseshoe	Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat	Peptidase M1, leukotriene A4 hydrolase/aminopeptidase C-terminal domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF09127	Leukotriene A4 hydrolase, C-terminal (Leuk-A4-hydro_C)	Leukotriene A4 hydrolase, C-terminal	-	Repeat
A, B, C, D	PF01433	Peptidase family M1 domain (Peptidase_M1)	Peptidase family M1 domain	Members of this family are aminopeptidases. The members differ widely in specificity, hydrolysing acidic, basic or neutral N-terminal residues. This family includes leukotriene-A4 hydrolase Swiss:P09960, this enzyme also has an aminopeptidase activ ...	Members of this family are aminopeptidases. The members differ widely in specificity, hydrolysing acidic, basic or neutral N-terminal residues. This family includes leukotriene-A4 hydrolase Swiss:P09960, this enzyme also has an aminopeptidase activity [1].	Domain
A, B, C, D	PF17900	Peptidase M1 N-terminal domain (Peptidase_M1_N)	Peptidase M1 N-terminal domain	This domain is found at the N-terminus of aminopeptidases from the M1 family.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	cold-active aminopeptidase	peptidase activity catalytic activity, acting on a protein metallopeptidase activity hydrolase activity catalytic activity cation binding transition metal ion binding zinc ion binding ion binding binding metal ion binding small molecule binding aminopeptidase activity exopeptidase activity	organic substance metabolic process organonitrogen compound metabolic process proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR034015	Aminopeptidase, leukotriene A4 hydrolase-like	Family
A, B, C, D	IPR001930	Peptidase M1, alanine aminopeptidase/leukotriene A4 hydrolase	Family
A, B, C, D	IPR016024	Armadillo-type fold	Homologous Superfamily
A, B, C, D	IPR015211	Peptidase M1, leukotriene A4 hydrolase/aminopeptidase C-terminal	Domain
A, B, C, D	IPR038502	Peptidase M1, LTA-4 hydrolase/aminopeptidase, C-terminal domain superfamily	Homologous Superfamily
A, B, C, D	IPR027268	Peptidase M4/M1, CTD superfamily	Homologous Superfamily
A, B, C, D	IPR014782	Peptidase M1, membrane alanine aminopeptidase	Domain
A, B, C, D	IPR045357	Aminopeptidase N-like , N-terminal domain	Domain
A, B, C, D	IPR042097	Aminopeptidase N-like , N-terminal domain superfamliy	Homologous Superfamily

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), 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.