Research workbench
Crystal structure of the G391V variant of human PGM-1
Analyse Crystal structure of the G391V 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
- 7S77
- Type
- protein
- Length
- 1,077 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.8
- Source
- Homo sapiens
- Molecule
- Phosphoglucomutase-1
- EC
- 5.4.2.2
- UniProt
- P36871
- Ligands
- SO4
- Pockets
- 11 · best druggability 0.69
Structure
x-ray diffraction · resolution 2.8 · 2 distinct chains · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoglucomutase-1 (EC 5.4.2.2) | protein | 548 | 38% helix, 26% strand | P36871 |
| B | Phosphoglucomutase-1 (EC 5.4.2.2) | protein | 529 | 36% helix, 24% strand | P36871 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 502 | 0.69 | 0.80 | 74 | empty |
| 2 | 271 | 0.69 | 0.84 | 43 | empty |
| 3 | 497 | 0.68 | 0.79 | 65 | SO4 |
| 4 | 473 | 0.63 | 0.76 | 57 | empty |
| 5 | 168 | 0.58 | 0.82 | 38 | empty |
Interfaces
1 interface between chains.
- A–B · 583 Ų buried · 10 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 7S77 · PDBe 7S77 · UniProt P36871
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