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Saccharomyces cerevisiae phosphoglycerate mutase

Analyse Saccharomyces cerevisiae phosphoglycerate mutase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4PGM
Type: protein
Length: 941 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphoglycerate mutase 1
EC: 5.4.2.1
UniProt: P00950
Pockets: 14 · best druggability 0.75

Structure

x-ray diffraction · 3 distinct chains · 43% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphoglycerate mutase 1 (EC 5.4.2.1)	protein	235	41% helix, 13% strand	P00950
B, D	Phosphoglycerate mutase 1 (EC 5.4.2.1)	protein	236	43% helix, 13% strand	P00950
C	Phosphoglycerate mutase 1 (EC 5.4.2.1)	protein	234	44% helix, 13% strand	P00950

Pockets

14 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	607	0.75	0.82	60	empty
2	549	0.75	0.82	59	empty
3	176	0.58	0.82	22	empty
4	164	0.58	0.83	23	empty
5	131	0.53	0.82	23	empty

Interfaces

6 interfaces between chains.

C–D · 957 Å² buried · 12 hydrogen bonds · protein-protein
A–B · 954 Å² buried · 12 hydrogen bonds · protein-protein
B–D · 921 Å² buried · 17 hydrogen bonds · protein-protein
A–C · 918 Å² buried · 18 hydrogen bonds · protein-protein
A–D · 61 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

4PGM · Saccharomyces cerevisiae phosphoglycerate mutase · the same entry in another collection · chain A against A, TM-score 1.00
P00950 · AlphaFold monomer V2.0 prediction for phosphoglycerate mutase 1 (P00950) · a predicted model of the same protein · chain C against A, TM-score 0.99

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P00950
Elsewhere: RCSB PDB 4PGM · PDBe 4PGM · UniProt P00950

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