5KM9

Human Histidine Triad Nucleotide Binding Protein 2 (hHint2) adenosine 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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B [auth A]	d5km9a_	Alpha and beta proteins (a+b)	HIT-like	HIT-like	HIT (HINT, histidine triad) family of protein kinase-interacting proteins	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A [auth B]	d5km9b_	Alpha and beta proteins (a+b)	HIT-like	HIT-like	HIT (HINT, histidine triad) family of protein kinase-interacting proteins	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B [auth A]	SCOP2B Superfamily	HIT-like	8100458	3000223	SCOP2B (2022-06-29)
A [auth B]	SCOP2B Superfamily	HIT-like	8100458	3000223	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)
B [auth A]	PF01230	e5km9A1	A: a+b three layers	X: HIT-like	H: HIT-related (From Topology)	T: HIT-related	F: PF01230	ECOD (1.6)
A [auth B]	PF01230	e5km9B1	A: a+b three layers	X: HIT-like	H: HIT-related (From Topology)	T: HIT-related	F: PF01230	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B [auth A]	3.30.428.10	Alpha Beta	2-Layer Sandwich	HIT family, subunit A	HIT-like	CATH (4.3.0)
A [auth B]	3.30.428.10	Alpha Beta	2-Layer Sandwich	HIT family, subunit A	HIT-like	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth B], B [auth A]	PF01230	HIT domain (HIT)	HIT domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth B], B [auth A]	Histidine triad nucleotide-binding protein 2, mitochondrial	binding nucleoside phosphate binding organic cyclic compound binding nucleotide binding heterocyclic compound binding small molecule binding hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides adenosine 5'-monophosphoramidase activity hydrolase activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds	lipid catabolic process organic substance metabolic process catabolic process primary metabolic process metabolic process organic substance catabolic process lipid metabolic process steroid metabolic process lipid biosynthetic process organic cyclic compound metabolic process biosynthetic process organic cyclic compound biosynthetic process organic substance biosynthetic process steroid biosynthetic process lipid catabolic process organic substance metabolic process catabolic process primary metabolic process metabolic process organic substance catabolic process lipid metabolic process steroid metabolic process lipid biosynthetic process organic cyclic compound metabolic process biosynthetic process organic cyclic compound biosynthetic process organic substance biosynthetic process steroid biosynthetic process peptidyl-lysine acetylation regulation of protein modification process peptidyl-lysine modification negative regulation of biological process protein acylation regulation of primary metabolic process peptidyl-amino acid modification negative regulation of protein modification process protein metabolic process protein modification process negative regulation of protein metabolic process negative regulation of macromolecule metabolic process regulation of biological process organonitrogen compound metabolic process regulation of protein metabolic process negative regulation of metabolic process biological regulation negative regulation of protein acetylation regulation of macromolecule metabolic process negative regulation of peptidyl-lysine acetylation protein acetylation regulation of protein acetylation macromolecule modification regulation of peptidyl-lysine acetylation macromolecule metabolic process regulation of metabolic process cellular process apoptotic process cell death programmed cell death	membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle mitochondrial membrane membrane organelle outer membrane organelle envelope bounding membrane of organelle mitochondrial envelope membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle mitochondrial membrane membrane organelle outer membrane organelle envelope bounding membrane of organelle mitochondrial envelope mitochondrial outer membrane outer membrane organelle membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth B], B [auth A]	IPR001310	Histidine triad (HIT) protein	Family
A [auth B], B [auth A]	IPR011146	HIT-like domain	Domain
A [auth B], B [auth A]	IPR036265	HIT-like superfamily	Homologous Superfamily
A [auth B], B [auth A]	IPR019808	Histidine triad, conserved site	Conserved Site

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A [auth B], B [auth A]	Pharos: Q9BX68	pancreatic ductal adenocarcinoma tuberculosis

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.