3IML

Crystal Structure Of S-Adenosylmethionine Synthetase From Burkholderia Pseudomallei

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d3imla1	Alpha and beta proteins (a+b)	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	automated matches	automated matches	Pseudomonas pseudomallei (Burkholderia pseudomallei ) [TaxId: 28450 ],	SCOPe (2.08)
A	d3imla4	Artifacts	Tags	Tags	Tags	N-terminal Tags	Pseudomonas pseudomallei (Burkholderia pseudomallei ) [TaxId: 28450 ],	SCOPe (2.08)
C	d3imlc1	Alpha and beta proteins (a+b)	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	automated matches	automated matches	Pseudomonas pseudomallei (Burkholderia pseudomallei ) [TaxId: 28450 ],	SCOPe (2.08)
D	d3imld1	Alpha and beta proteins (a+b)	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	automated matches	automated matches	Pseudomonas pseudomallei (Burkholderia pseudomallei ) [TaxId: 28450 ],	SCOPe (2.08)
B	d3imlb1	Alpha and beta proteins (a+b)	S-adenosylmethionine synthetase	S-adenosylmethionine synthetase	automated matches	automated matches	Pseudomonas pseudomallei (Burkholderia pseudomallei ) [TaxId: 28450 ],	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	S-AdoMet_synt_C	e3imlA4	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: S-AdoMet_synt_C	ECOD (1.6)
A	S-AdoMet_synt_M	e3imlA5	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: S-AdoMet_synt_M	ECOD (1.6)
A	S-AdoMet_synt_N	e3imlA6	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: S-AdoMet_synt_N	ECOD (1.6)
C	S-AdoMet_synt_C	e3imlC4	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: S-AdoMet_synt_C	ECOD (1.6)
C	S-AdoMet_synt_M	e3imlC5	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: S-AdoMet_synt_M	ECOD (1.6)
C	S-AdoMet_synt_N	e3imlC6	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: S-AdoMet_synt_N	ECOD (1.6)
D	S-AdoMet_synt_C	e3imlD4	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: S-AdoMet_synt_C	ECOD (1.6)
D	S-AdoMet_synt_M	e3imlD5	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: S-AdoMet_synt_M	ECOD (1.6)
D	S-AdoMet_synt_N	e3imlD3	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: S-AdoMet_synt_N	ECOD (1.6)
B	S-AdoMet_synt_C	e3imlB1	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: S-AdoMet_synt_C	ECOD (1.6)
B	S-AdoMet_synt_M	e3imlB4	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: S-AdoMet_synt_M	ECOD (1.6)
B	S-AdoMet_synt_N	e3imlB5	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: S-adenosylmethionine synthetase (From Topology)	T: S-adenosylmethionine synthetase	F: S-AdoMet_synt_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
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)
D	3.30.300.10	Alpha Beta	2-Layer Sandwich	GMP Synthetase	Chain A, domain 3	CATH (4.3.0)
B	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 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	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
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
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

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.