2VZE

Crystal structure of human acyl-CoA synthetase medium-chain family member 2A (L64P mutation) in complex with AMP

External Resource: Annotation

Domain Annotation: SCOP/SCOPe 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)
A	d2vzea_	Multi-domain proteins (alpha and beta)	Acetyl-CoA synthetase-like	Acetyl-CoA synthetase-like	automated matches	automated matches	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d2vzeb_	Multi-domain proteins (alpha and beta)	Acetyl-CoA synthetase-like	Acetyl-CoA synthetase-like	automated matches	automated matches	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d2vzec_	Multi-domain proteins (alpha and beta)	Acetyl-CoA synthetase-like	Acetyl-CoA synthetase-like	automated matches	automated matches	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	AMP-binding_3rd	e2vzeA4	A: beta barrels	X: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	H: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	T: beta-barrel domain in acetyl-CoA synthetase-like proteins	F: AMP-binding_3rd	ECOD (1.6)
A	AMP-binding_C	e2vzeA3	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: a+b domain in acetyl-CoA synthetase-like proteins (From Topology)	T: a+b domain in acetyl-CoA synthetase-like proteins	F: AMP-binding_C	ECOD (1.6)
A	AMP-binding_1st	e2vzeA2	A: a/b three-layered sandwiches	X: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	T: Rossmann-like domain in Acetyl-CoA synthetase-like proteins	F: AMP-binding_1st	ECOD (1.6)
A	AMP-binding_2nd	e2vzeA1	A: a/b three-layered sandwiches	X: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	T: Rossmann-like domain in Acetyl-CoA synthetase-like proteins	F: AMP-binding_2nd	ECOD (1.6)
B	AMP-binding_3rd	e2vzeB1	A: beta barrels	X: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	H: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	T: beta-barrel domain in acetyl-CoA synthetase-like proteins	F: AMP-binding_3rd	ECOD (1.6)
B	AMP-binding_C	e2vzeB2	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: a+b domain in acetyl-CoA synthetase-like proteins (From Topology)	T: a+b domain in acetyl-CoA synthetase-like proteins	F: AMP-binding_C	ECOD (1.6)
B	AMP-binding_1st	e2vzeB4	A: a/b three-layered sandwiches	X: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	T: Rossmann-like domain in Acetyl-CoA synthetase-like proteins	F: AMP-binding_1st	ECOD (1.6)
B	AMP-binding_2nd	e2vzeB3	A: a/b three-layered sandwiches	X: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	T: Rossmann-like domain in Acetyl-CoA synthetase-like proteins	F: AMP-binding_2nd	ECOD (1.6)
C	AMP-binding_3rd	e2vzeC1	A: beta barrels	X: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	H: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	T: beta-barrel domain in acetyl-CoA synthetase-like proteins	F: AMP-binding_3rd	ECOD (1.6)
C	AMP-binding_C	e2vzeC2	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: a+b domain in acetyl-CoA synthetase-like proteins (From Topology)	T: a+b domain in acetyl-CoA synthetase-like proteins	F: AMP-binding_C	ECOD (1.6)
C	AMP-binding_1st	e2vzeC4	A: a/b three-layered sandwiches	X: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	T: Rossmann-like domain in Acetyl-CoA synthetase-like proteins	F: AMP-binding_1st	ECOD (1.6)
C	AMP-binding_2nd	e2vzeC3	A: a/b three-layered sandwiches	X: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	T: Rossmann-like domain in Acetyl-CoA synthetase-like proteins	F: AMP-binding_2nd	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.12780	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	ANL, N-terminal domain	CATH (4.3.0)
A	3.30.300.30	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (4.3.0)
B	3.40.50.12780	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	ANL, N-terminal domain	CATH (4.3.0)
B	3.30.300.30	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (4.3.0)
C	3.40.50.12780	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	ANL, N-terminal domain	CATH (4.3.0)
C	3.30.300.30	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF00501	AMP-binding enzyme (AMP-binding)	AMP-binding enzyme	-	Family
A, B, C	PF13193	AMP-binding enzyme C-terminal domain (AMP-binding_C)	AMP-binding enzyme C-terminal domain	This is a small domain that is found C terminal to Pfam:PF00501. It has a central beta sheet core that is flanked by alpha helices.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	ACYL-COENZYME A SYNTHETASE ACSM2A, MITOCHONDRIAL	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding fatty acid ligase activity ligase activity, forming carbon-sulfur bonds catalytic activity acid-thiol ligase activity ligase activity ATP-dependent activity fatty-acyl-CoA synthase activity acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity C-acyltransferase activity decanoate-CoA ligase activity CoA-ligase activity medium-chain fatty acid-CoA ligase activity fatty acid-CoA ligase activity benzoate-CoA ligase activity cation binding metal ion binding	nucleoside phosphate metabolic process cellular metabolic process primary metabolic process purine-containing compound metabolic process nucleobase-containing compound metabolic process acyl-CoA metabolic process organophosphate metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process metabolic process sulfur compound metabolic process cellular process small molecule metabolic process amide metabolic process nucleoside phosphate metabolic process cellular metabolic process primary metabolic process purine-containing compound metabolic process nucleobase-containing compound metabolic process acyl-CoA metabolic process organophosphate metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process metabolic process sulfur compound metabolic process cellular process small molecule metabolic process amide metabolic process thioester metabolic process phosphorus metabolic process fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid metabolic process cellular biosynthetic process carboxylic acid metabolic process lipid biosynthetic process organic acid biosynthetic process organic acid metabolic process fatty acid biosynthetic process carboxylic acid biosynthetic process biosynthetic process cellular lipid metabolic process monocarboxylic acid metabolic process lipid metabolic process chemical homeostasis homeostatic process triglyceride homeostasis acylglycerol homeostasis lipid homeostasis fatty acid derivative metabolic process medium-chain fatty-acyl-CoA metabolic process fatty-acyl-CoA metabolic process glucose homeostasis carbohydrate homeostasis	membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle membrane-enclosed lumen mitochondrial matrix intracellular organelle lumen organelle lumen

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR051087	Mitochondrial Acyl-CoA Synthetase Medium-Chain	Family
A, B, C	IPR020845	AMP-binding, conserved site	Conserved Site
A, B, C	IPR045851	AMP-binding enzyme, C-terminal domain superfamily	Homologous Superfamily
A, B, C	IPR042099	ANL, N-terminal domain	Homologous Superfamily
A, B, C	IPR025110	AMP-binding enzyme, C-terminal domain	Domain
A, B, C	IPR000873	AMP-dependent synthetase/ligase domain	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C	Pharos: Q08AH3	chronic kidney disease nephrolithiasis gout hypertensive disorder

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.