6S83

Crystal structure of methionine adenosyltransferase from Pyrococcus furiosus in complex with AMPPCP, SAM, and PCP

External Resource: Annotation

Domain Annotation: ECOD Classification
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	AdoMet_Synthase	e6s83C1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: AdoMet_Synthase	ECOD (1.6)
F	AdoMet_Synthase	e6s83F1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: AdoMet_Synthase	ECOD (1.6)
A	AdoMet_Synthase	e6s83A1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: AdoMet_Synthase	ECOD (1.6)
B	AdoMet_Synthase	e6s83B1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: AdoMet_Synthase	ECOD (1.6)
D	AdoMet_Synthase	e6s83D1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: AdoMet_Synthase	ECOD (1.6)
E	AdoMet_Synthase	e6s83E1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: AdoMet_Synthase	ECOD (1.6)
G	AdoMet_Synthase	e6s83G1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: AdoMet_Synthase	ECOD (1.6)
H	AdoMet_Synthase	e6s83H1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: AdoMet_Synthase	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F, G, H	PF01941	S-adenosylmethionine synthetase (AdoMet synthetase) (AdoMet_Synthase)	S-adenosylmethionine synthetase (AdoMet synthetase)	-	Family

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, G, H	S-adenosylmethionine synthase	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding methionine adenosyltransferase activity transferase activity transferase activity, transferring alkyl or aryl (other than methyl) groups catalytic activity	sulfur compound biosynthetic process biosynthetic process S-adenosylmethionine biosynthetic process S-adenosylmethionine metabolic process sulfur compound metabolic process metabolic process cellular process small molecule metabolic process one-carbon metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H	IPR027790	S-adenosylmethionine synthase	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR002795	S-adenosylmethionine synthetase, archaea	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR042544	S-adenosylmethionine synthetase, domain 3	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 R01GM157729.