Annotations: 1P7L

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d1p7lb1	Alpha and beta proteins (a+b)	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
D	d1p7ld1	Alpha and beta proteins (a+b)	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1p7la1	Alpha and beta proteins (a+b)	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C	d1p7lc1	Alpha and beta proteins (a+b)	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	S-adenosylmethionine synthetase	8036387	3000766	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	S-adenosylmethionine synthetase	8036385	3000766	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	S-adenosylmethionine synthetase	8036388	3000766	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	S-adenosylmethionine synthetase	8036385	3000766	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	S-adenosylmethionine synthetase	8036388	3000766	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	S-adenosylmethionine synthetase	8036387	3000766	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	S-adenosylmethionine synthetase	8036388	3000766	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	S-adenosylmethionine synthetase	8036385	3000766	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	S-adenosylmethionine synthetase	8036387	3000766	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	S-adenosylmethionine synthetase	8036387	3000766	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	S-adenosylmethionine synthetase	8036385	3000766	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	S-adenosylmethionine synthetase	8036388	3000766	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	PF00438	e1p7lB1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF00438	ECOD (1.6)
B	PF02772	e1p7lB2	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF02772	ECOD (1.6)
B	PF02773	e1p7lB3	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF02773	ECOD (1.6)
D	PF00438	e1p7lD1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF00438	ECOD (1.6)
D	PF02772	e1p7lD2	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF02772	ECOD (1.6)
D	PF02773	e1p7lD3	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF02773	ECOD (1.6)
A	PF00438	e1p7lA1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF00438	ECOD (1.6)
A	PF02772	e1p7lA2	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF02772	ECOD (1.6)
A	PF02773	e1p7lA3	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF02773	ECOD (1.6)
C	PF00438	e1p7lC1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF00438	ECOD (1.6)
C	PF02772	e1p7lC2	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF02772	ECOD (1.6)
C	PF02773	e1p7lC3	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: PF02773	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.30.300.10	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (4.3.0)
D	3.30.300.10	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (4.3.0)
A	3.30.300.10	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (4.3.0)
C	3.30.300.10	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, D	PF00438	S-adenosylmethionine synthetase, N-terminal domain (S-AdoMet_synt_N)	S-adenosylmethionine synthetase, N-terminal domain	The three domains of S-adenosylmethionine synthetase have the same alpha+beta fold.	Domain
A, B, C, D	PF02773	S-adenosylmethionine synthetase, C-terminal domain (S-AdoMet_synt_C)	S-adenosylmethionine synthetase, C-terminal domain	The three domains of S-adenosylmethionine synthetase have the same alpha+beta fold.	Domain
A, B, C, D	PF02772	S-adenosylmethionine synthetase, central domain (S-AdoMet_synt_M)	S-adenosylmethionine synthetase, central domain	The three domains of S-adenosylmethionine synthetase have the same alpha+beta fold.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	S-adenosylmethionine synthetase	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 potassium ion binding alkali metal ion binding methionine adenosyltransferase activity transferase activity transferase activity, transferring alkyl or aryl (other than methyl) groups catalytic activity identical protein binding protein binding	S-adenosylmethionine cycle organic substance metabolic process S-adenosylmethionine metabolic process cellular metabolic process sulfur compound metabolic process metabolic process cellular process small molecule metabolic process one-carbon metabolic process cellular biosynthetic process sulfur compound biosynthetic process biosynthetic process S-adenosylmethionine biosynthetic process organic substance biosynthetic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR022636	S-adenosylmethionine synthetase superfamily	Homologous Superfamily
A, B, C, D	IPR022629	S-adenosylmethionine synthetase, central domain	Domain
A, B, C, D	IPR022628	S-adenosylmethionine synthetase, N-terminal	Domain
A, B, C, D	IPR022631	S-adenosylmethionine synthetase, conserved site	Conserved Site
A, B, C, D	IPR022630	S-adenosylmethionine synthetase, C-terminal	Domain
A, B, C, D	IPR002133	S-adenosylmethionine synthetase	Family

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.