Research workbench
Crystal structure of the G291R mutant of human phosphoglucomutase 1
Analyse Crystal structure of the G291R mutant of human phosphoglucomutase 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HSH
- Type
- protein
- Length
- 1,063 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
- SO4
- Pockets
- 11 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoglucomutase-1 (EC 5.4.2.2) | protein | 535 | 38% helix, 25% strand | P36871 |
| B | Phosphoglucomutase-1 (EC 5.4.2.2) | protein | 528 | 38% helix, 25% strand | P36871 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 359 | 0.72 | 0.84 | 69 | empty |
| 2 | 413 | 0.64 | 0.79 | 72 | SO4 |
| 3 | 67 | 0.64 | 0.92 | 27 | empty |
| 4 | 439 | 0.63 | 0.77 | 53 | SO4 |
| 5 | 332 | 0.60 | 0.78 | 54 | empty |
Interfaces
1 interface between chains.
- A–B · 538 Ų buried · 11 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 5HSH · PDBe 5HSH · UniProt P36871
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.