6H91

Phosphorylated beta-phosphoglucomutase from Lactococcus lactis in an open conformer to 2.4 A

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Protein Modification Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d6h91b_	Alpha and beta proteins (a/b)	HAD-like	HAD-like	beta-Phosphoglucomutase-like	beta-Phosphoglucomutase	(Lactococcus lactis subsp. lactis Il1403 ) [TaxId: 272623 ],	SCOPe (2.08)
A	d6h91a_	Alpha and beta proteins (a/b)	HAD-like	HAD-like	beta-Phosphoglucomutase-like	beta-Phosphoglucomutase	(Lactococcus lactis subsp. lactis Il1403 ) [TaxId: 272623 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	HAD-like	8033801	3001890	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	HAD-like	8033801	3001890	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	HAD_2	e6h91B1	A: a/b three-layered sandwiches	X: HAD domain-like	H: HAD domain-related	T: HAD-like	F: HAD_2	ECOD (1.6)
A	HAD_2	e6h91A1	A: a/b three-layered sandwiches	X: HAD domain-like	H: HAD domain-related	T: HAD-like	F: HAD_2	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00702	haloacid dehalogenase-like hydrolase (Hydrolase)	haloacid dehalogenase-like hydrolase	This family is structurally different from the alpha/beta hydrolase family (Pfam:PF00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted fo ...	This family is structurally different from the alpha/beta hydrolase family (Pfam:PF00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain [1]. Those members with the characteristic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Beta-phosphoglucomutase	beta-phosphoglucomutase activity isomerase activity intramolecular phosphotransferase activity catalytic activity intramolecular transferase activity cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding	carbohydrate metabolic process primary metabolic process metabolic process cellular process	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR010972	Beta-phosphoglucomutase	Family
A, B	IPR036412	HAD-like superfamily	Homologous Superfamily
A, B	IPR023214	HAD superfamily	Homologous Superfamily
A, B	IPR051600	Beta-phosphoglucomutase-like	Family
A, B	IPR006439	HAD hydrolase, subfamily IA	Family
A, B	IPR010976	Beta-phosphoglucomutase hydrolase	Domain
A, B	IPR023198	Phosphoglycolate phosphatase-like, domain 2	Homologous Superfamily

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A, B	PHD	Parent Component: ASP RESID: AA0033 PSI-MOD : L-aspartic 4-phosphoric anhydride MOD:00042

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.