3PMG

STRUCTURE OF RABBIT MUSCLE PHOSPHOGLUCOMUTASE AT 2.4 ANGSTROMS RESOLUTION. USE OF FREEZING POINT DEPRESSANT AND REDUCED TEMPERATURE TO ENHANCE DIFFRACTIVITY

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Protein Modification Annotation
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d3pmga2	Alpha and beta proteins (a/b)	Phosphoglucomutase, first 3 domains	Phosphoglucomutase, first 3 domains	Phosphoglucomutase, first 3 domains	Phosphoglucomutase, middle and C-terminal domain	(Oryctolagus cuniculus ) [TaxId: 9986 ],	SCOPe (2.08)
A	d3pmga1	Alpha and beta proteins (a/b)	Phosphoglucomutase, first 3 domains	Phosphoglucomutase, first 3 domains	Phosphoglucomutase, first 3 domains	Phosphoglucomutase, N-terminal domain	(Oryctolagus cuniculus ) [TaxId: 9986 ],	SCOPe (2.08)
A	d3pmga4	Alpha and beta proteins (a+b)	TBP-like	Phosphoglucomutase, C-terminal domain	Phosphoglucomutase, C-terminal domain	Phosphoglucomutase	(Oryctolagus cuniculus ) [TaxId: 9986 ],	SCOPe (2.08)
B	d3pmgb2	Alpha and beta proteins (a/b)	Phosphoglucomutase, first 3 domains	Phosphoglucomutase, first 3 domains	Phosphoglucomutase, first 3 domains	Phosphoglucomutase, middle and C-terminal domain	(Oryctolagus cuniculus ) [TaxId: 9986 ],	SCOPe (2.08)
B	d3pmgb1	Alpha and beta proteins (a/b)	Phosphoglucomutase, first 3 domains	Phosphoglucomutase, first 3 domains	Phosphoglucomutase, first 3 domains	Phosphoglucomutase, N-terminal domain	(Oryctolagus cuniculus ) [TaxId: 9986 ],	SCOPe (2.08)
B	d3pmgb4	Alpha and beta proteins (a+b)	TBP-like	Phosphoglucomutase, C-terminal domain	Phosphoglucomutase, C-terminal domain	Phosphoglucomutase	(Oryctolagus cuniculus ) [TaxId: 9986 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Phosphoglucomutase first 3 domains	8020680	4000812	SCOP2 (2022-06-29)
A	SCOP2 Family	Phosphoglucomutase first 3 domains	8020682	4000812	SCOP2 (2022-06-29)
A	SCOP2 Family	Phosphoglucomutase first 3 domains	8020683	4000812	SCOP2 (2022-06-29)
A	SCOP2 Family	Phosphoglucomutase C-terminal domain-like	8023982	4002037	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Phosphoglucomutase first 3 domains	8033060	3001532	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Phosphoglucomutase first 3 domains	8033062	3001532	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Phosphoglucomutase first 3 domains	8033063	3001532	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Phosphoglucomutase C-terminal domain-like	8036361	3000732	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Phosphoglucomutase first 3 domains	8033063	3001532	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Phosphoglucomutase first 3 domains	8033060	3001532	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Phosphoglucomutase first 3 domains	8033062	3001532	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Phosphoglucomutase C-terminal domain-like	8036361	3000732	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	PGM_PMM_IV_1	e3pmgA1	A: a+b two layers	X: TBP-like	H: Phosphoglucomutase, C-terminal domain (From Topology)	T: Phosphoglucomutase, C-terminal domain	F: PGM_PMM_IV_1	ECOD (1.6)
A	PGM_PMM_I	e3pmgA2	A: a/b three-layered sandwiches	X: Phosphoglucomutase, first 3 domains (From Topology)	H: Phosphoglucomutase, first 3 domains (From Topology)	T: Phosphoglucomutase, first 3 domains	F: PGM_PMM_I	ECOD (1.6)
A	PGM_PMM_II	e3pmgA3	A: a/b three-layered sandwiches	X: Phosphoglucomutase, first 3 domains (From Topology)	H: Phosphoglucomutase, first 3 domains (From Topology)	T: Phosphoglucomutase, first 3 domains	F: PGM_PMM_II	ECOD (1.6)
A	PGM_PMM_III_1	e3pmgA4	A: a/b three-layered sandwiches	X: Phosphoglucomutase, first 3 domains (From Topology)	H: Phosphoglucomutase, first 3 domains (From Topology)	T: Phosphoglucomutase, first 3 domains	F: PGM_PMM_III_1	ECOD (1.6)
B	PGM_PMM_IV_1	e3pmgB1	A: a+b two layers	X: TBP-like	H: Phosphoglucomutase, C-terminal domain (From Topology)	T: Phosphoglucomutase, C-terminal domain	F: PGM_PMM_IV_1	ECOD (1.6)
B	PGM_PMM_I	e3pmgB2	A: a/b three-layered sandwiches	X: Phosphoglucomutase, first 3 domains (From Topology)	H: Phosphoglucomutase, first 3 domains (From Topology)	T: Phosphoglucomutase, first 3 domains	F: PGM_PMM_I	ECOD (1.6)
B	PGM_PMM_II	e3pmgB3	A: a/b three-layered sandwiches	X: Phosphoglucomutase, first 3 domains (From Topology)	H: Phosphoglucomutase, first 3 domains (From Topology)	T: Phosphoglucomutase, first 3 domains	F: PGM_PMM_II	ECOD (1.6)
B	PGM_PMM_III_1	e3pmgB4	A: a/b three-layered sandwiches	X: Phosphoglucomutase, first 3 domains (From Topology)	H: Phosphoglucomutase, first 3 domains (From Topology)	T: Phosphoglucomutase, first 3 domains	F: PGM_PMM_III_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.120.10	Alpha Beta	3-Layer(aba) Sandwich	Alpha-D-Glucose-1,6-Bisphosphate	Chain A, domain 3	CATH (4.3.0)
A	3.30.310.50	Alpha Beta	2-Layer Sandwich	TATA-Binding Protein	Alpha-D-phosphohexomutase, C-terminal domain	CATH (4.3.0)
B	3.40.120.10	Alpha Beta	3-Layer(aba) Sandwich	Alpha-D-Glucose-1,6-Bisphosphate	Chain A, domain 3	CATH (4.3.0)
B	3.30.310.50	Alpha Beta	2-Layer Sandwich	TATA-Binding Protein	Alpha-D-phosphohexomutase, C-terminal domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF02878	Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I (PGM_PMM_I)	Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I	-	Domain
A, B	PF02879	Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II (PGM_PMM_II)	Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II	-	Domain
A, B	PF02880	Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III (PGM_PMM_III)	Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Phosphoglucomutase-1	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding phosphoglucomutase activity isomerase activity intramolecular phosphotransferase activity catalytic activity intramolecular transferase activity	monosaccharide metabolic process carbohydrate metabolic process organic substance metabolic process hexose metabolic process small molecule metabolic process metabolic process primary metabolic process glucose metabolic process	membrane-bounded organelle intracellular anatomical structure cellular anatomical entity intracellular membrane-bounded organelle endomembrane system sarcoplasm intracellular organelle organelle endoplasmic reticulum sarcoplasmic reticulum cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR005845	Alpha-D-phosphohexomutase, alpha/beta/alpha domain II	Domain
A, B	IPR016055	Alpha-D-phosphohexomutase, alpha/beta/alpha I/II/III	Homologous Superfamily
A, B	IPR016066	Alpha-D-phosphohexomutase, conserved site	Conserved Site
A, B	IPR005844	Alpha-D-phosphohexomutase, alpha/beta/alpha domain I	Domain
A, B	IPR045244	Phosphoglucomutase	Family
A, B	IPR005841	Alpha-D-phosphohexomutase superfamily	Family
A, B	IPR036900	Alpha-D-phosphohexomutase, C-terminal domain superfamily	Homologous Superfamily
A, B	IPR005846	Alpha-D-phosphohexomutase, alpha/beta/alpha domain III	Domain

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A, B	SEP	Parent Component: SER RESID: AA0037 PSI-MOD : O-phospho-L-serine MOD:00046

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
B	phosphoglucomutase M-CSA #352	Phosphoglucomutase catalyses the transfer of a phosphate fragment between the 1- and 6-O atoms of glucose. As suggested by the enzyme's name, in its stable form it exists esterified, at the gamma-hydroxyl group of Ser116. The enzyme is involved in the glycogenolysis pathway. Once a 1-phosphate glucose molecule is released from glycogen by glycogen phosphorylase, phosphoglucomutase catalyses the interconversion of this relatively useless metabolic intermediate into 6-phosphate glucose. This metabolite can then be utilised in multiple cellular pathways including the glycolytic, pentose phosphate or biosynthetic pathways. When glucose levels are high, phosphoglucomutase can act in the opposite fashion, converting 6-phosphate glucose to 1-phosphate glucose. In combination with UDP-glucose-pyrophosphorylase and glycogen synthase, this change in equilibrium will result in the reformation of the 1-phosphate glucose monomer with a glycogen polymer.	Defined by 7 residues: SER:B-116HIS:B-117ASP:B-287ASP:B-289ASP:B-291ARG:B-292LYS:B-388 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 5.4.2.2 (PDB Primary Data) Search M-CSA Motif + EC 5.4.2.2

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.