Research workbench
Crystal structure of the T337M variant of human pgm-1
Analyse Crystal structure of the T337M variant of human pgm-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7S0W
- Type
- protein
- Length
- 1,056 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoglucomutase-1
- EC
- 5.4.2.2
- UniProt
- P36871
- Ligands
- CO, SO4
- Pockets
- 7 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoglucomutase-1 (EC 5.4.2.2) | protein | 557 | 38% helix, 25% strand | P36871 |
| B | Phosphoglucomutase-1 (EC 5.4.2.2) | protein | 499 | 35% helix, 23% strand | P36871 |
Ligands and binding sites
- CO · Cobalt (II) ion · metal · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 13 copies · chains A, B
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 591 | 0.70 | 0.78 | 75 | SO4 |
| 2 | 520 | 0.64 | 0.76 | 61 | empty |
| 3 | 282 | 0.61 | 0.80 | 43 | SO4 |
| 4 | 274 | 0.55 | 0.76 | 33 | empty |
| 5 | 67 | 0.30 | 0.74 | 19 | SO4 |
Interfaces
1 interface between chains.
- A–B · 490 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
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 P36871
- Elsewhere: RCSB PDB 7S0W · PDBe 7S0W · UniProt P36871
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