2WVM

H309A mutant of Mannosyl-3-phosphoglycerate synthase from Thermus thermophilus HB27 in complex with GDP-alpha-D-Mannose and Mg(II)

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Nucleotide-diphospho-sugar transferases	8053966	3000077	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Nucleotide-diphospho-sugar transferases	8053966	3000077	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)
A	Osmo_MPGsynth	e2wvmA1	A: a/b three-layered sandwiches	X: Nucleotide-diphospho-sugar transferases (From Topology)	H: Nucleotide-diphospho-sugar transferases (From Topology)	T: Nucleotide-diphospho-sugar transferases	F: Osmo_MPGsynth	ECOD (1.6)
B	Osmo_MPGsynth	e2wvmB1	A: a/b three-layered sandwiches	X: Nucleotide-diphospho-sugar transferases (From Topology)	H: Nucleotide-diphospho-sugar transferases (From Topology)	T: Nucleotide-diphospho-sugar transferases	F: Osmo_MPGsynth	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.550.10	Alpha Beta	Alpha-Beta Complex	Spore Coat Polysaccharide Biosynthesis Protein SpsA	Chain A	CATH (4.3.0)
B	3.90.550.10	Alpha Beta	Alpha-Beta Complex	Spore Coat Polysaccharide Biosynthesis Protein SpsA	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF09488	Mannosyl-3-phosphoglycerate synthase (osmo_MPGsynth) (Osmo_MPGsynth)	Mannosyl-3-phosphoglycerate synthase (osmo_MPGsynth)	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	MANNOSYL-3-PHOSPHOGLYCERATE SYNTHASE	glycosyltransferase activity transferase activity hexosyltransferase activity catalytic activity mannosyl-3-phosphoglycerate synthase activity cation binding ion binding binding metal ion binding small molecule binding	carbohydrate derivative biosynthetic process carbohydrate metabolic process glycosyl compound metabolic process glycosyl compound biosynthetic process small molecule biosynthetic process oxoacid metabolic process glycoside metabolic process carbohydrate biosynthetic process carboxylic acid metabolic process carbohydrate derivative metabolic process primary metabolic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process glycoside biosynthetic process carbohydrate derivative biosynthetic process carbohydrate metabolic process glycosyl compound metabolic process glycosyl compound biosynthetic process small molecule biosynthetic process oxoacid metabolic process glycoside metabolic process carbohydrate biosynthetic process carboxylic acid metabolic process carbohydrate derivative metabolic process primary metabolic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process glycoside biosynthetic process mannosylglycerate biosynthetic process biosynthetic process small molecule metabolic process metabolic process cellular process mannosylglycerate metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR012812	Mannosyl-3-phosphoglycerate synthase	Family
A, B	IPR029044	Nucleotide-diphospho-sugar transferases	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.