2WH5

Crystal structure of human acyl-CoA binding domain 4 complexed with stearoyl-CoA

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)
E	d2wh5e_	All alpha proteins	Acyl-CoA binding protein-like	Acyl-CoA binding protein	automated matches	automated matches	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d2wh5a_	All alpha proteins	Acyl-CoA binding protein-like	Acyl-CoA binding protein	automated matches	automated matches	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d2wh5b_	All alpha proteins	Acyl-CoA binding protein-like	Acyl-CoA binding protein	automated matches	automated matches	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d2wh5c_	All alpha proteins	Acyl-CoA binding protein-like	Acyl-CoA binding protein	automated matches	automated matches	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d2wh5d_	All alpha proteins	Acyl-CoA binding protein-like	Acyl-CoA binding protein	automated matches	automated matches	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
F	d2wh5f_	All alpha proteins	Acyl-CoA binding protein-like	Acyl-CoA binding protein	automated matches	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)
E	SCOP2B Superfamily	Acyl-CoA binding protein	8073176	3001219	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Acyl-CoA binding protein	8073176	3001219	SCOP2B (2022-06-29)
B	SCOP2 Family	Acyl-CoA binding protein	8073175	4000745	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	Acyl-CoA binding protein	8073176	3001219	SCOP2 (2022-06-29)
C	SCOP2B Superfamily	Acyl-CoA binding protein	8073176	3001219	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Acyl-CoA binding protein	8073176	3001219	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Acyl-CoA binding protein	8073176	3001219	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)
E	ACBP	e2wh5E1	A: alpha bundles	X: Acyl-CoA binding protein-like (From Topology)	H: Acyl-CoA binding protein-like (From Topology)	T: Acyl-CoA binding protein-like	F: ACBP	ECOD (1.6)
A	ACBP	e2wh5A1	A: alpha bundles	X: Acyl-CoA binding protein-like (From Topology)	H: Acyl-CoA binding protein-like (From Topology)	T: Acyl-CoA binding protein-like	F: ACBP	ECOD (1.6)
B	ACBP	e2wh5B1	A: alpha bundles	X: Acyl-CoA binding protein-like (From Topology)	H: Acyl-CoA binding protein-like (From Topology)	T: Acyl-CoA binding protein-like	F: ACBP	ECOD (1.6)
C	ACBP	e2wh5C1	A: alpha bundles	X: Acyl-CoA binding protein-like (From Topology)	H: Acyl-CoA binding protein-like (From Topology)	T: Acyl-CoA binding protein-like	F: ACBP	ECOD (1.6)
D	ACBP	e2wh5D1	A: alpha bundles	X: Acyl-CoA binding protein-like (From Topology)	H: Acyl-CoA binding protein-like (From Topology)	T: Acyl-CoA binding protein-like	F: ACBP	ECOD (1.6)
F	ACBP	e2wh5F1	A: alpha bundles	X: Acyl-CoA binding protein-like (From Topology)	H: Acyl-CoA binding protein-like (From Topology)	T: Acyl-CoA binding protein-like	F: ACBP	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
E	1.20.80.10	Mainly Alpha	Up-down Bundle	Acyl-CoA Binding Protein		CATH (4.3.0)
A	1.20.80.10	Mainly Alpha	Up-down Bundle	Acyl-CoA Binding Protein		CATH (4.3.0)
B	1.20.80.10	Mainly Alpha	Up-down Bundle	Acyl-CoA Binding Protein		CATH (4.3.0)
C	1.20.80.10	Mainly Alpha	Up-down Bundle	Acyl-CoA Binding Protein		CATH (4.3.0)
D	1.20.80.10	Mainly Alpha	Up-down Bundle	Acyl-CoA Binding Protein		CATH (4.3.0)
F	1.20.80.10	Mainly Alpha	Up-down Bundle	Acyl-CoA Binding Protein		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	PF00887	Acyl CoA binding protein (ACBP)	Acyl CoA binding protein	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	ACYL-COA-BINDING DOMAIN-CONTAINING PROTEIN 4	amide binding binding fatty-acyl-CoA binding acyl-CoA binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding lipid binding heterocyclic compound binding fatty acid derivative binding small molecule binding sulfur compound binding	fatty acid metabolic process oxoacid metabolic process carboxylic acid metabolic process primary metabolic process metabolic process cellular process small molecule metabolic process monocarboxylic acid metabolic process organic acid metabolic process lipid metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR022408	Acyl-CoA-binding protein, ACBP, conserved site	Conserved Site
A, B, C, D, E A, B, C, D, E, F	IPR000582	Acyl-CoA-binding protein, ACBP	Domain
A, B, C, D, E A, B, C, D, E, F	IPR035984	Acyl-CoA binding protein superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR014352	FERM/acyl-CoA-binding protein superfamily	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D, E A, B, C, D, E, F	Pharos: Q8NC06	Liver Cirrhosis, Experimental hypertensive disorder hypothyroidism

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 R01GM157729.