Research workbench
E.COLI cofactor-dependent phosphoglycerate mutase
Analyse E.COLI cofactor-dependent phosphoglycerate mutase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1E58
- Type
- protein
- Length
- 247 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoglycerate mutase
- EC
- 5.4.2.1
- UniProt
- P62707
- Ligands
- SO4, CL
- Pockets
- 4 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoglycerate mutase (EC 5.4.2.1) | protein | 247 | 44% helix, 14% strand | P62707 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 406 | 0.75 | 0.85 | 42 | SO4 |
| 2 | 74 | 0.38 | 0.77 | 16 | empty |
| 3 | 73 | 0.36 | 0.76 | 14 | empty |
| 4 | 85 | 0.34 | 0.74 | 14 | empty |
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 1E58 · E.coli cofactor-dependent phosphoglycerate mutase · the same entry in another collection · chain A against A, TM-score 1.00
- P62707 · AlphaFold monomer V2.0 prediction for 2,3-bisphosphoglycerate- dependent phosphoglycerate… · a predicted model of the same protein · chain A 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 P62707
- Elsewhere: RCSB PDB 1E58 · PDBe 1E58 · UniProt P62707
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