Research workbench
Crystal structure of wild-type human phosphoglucomutase 1 in complex with glucose-6-phosphate
Analyse Crystal structure of wild-type human phosphoglucomutase 1 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6UIQ
- Type
- protein
- Length
- 1,128 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
- G6P, MG
- Pockets
- 9 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A | Phosphoglucomutase-1 (EC 5.4.2.2) | protein | 564 | 37% helix, 25% strand | P36871 |
Ligands and binding sites
- G6P · 6-O-phosphono-alpha-D-glucopyranose · sugar · 2 copies · chains B, A
- MG · Magnesium ion · metal · 2 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 842 | 0.74 | 0.79 | 80 | G6P |
| 2 | 790 | 0.74 | 0.79 | 83 | G6P |
| 3 | 507 | 0.63 | 0.76 | 59 | empty |
| 4 | 125 | 0.44 | 0.76 | 26 | empty |
| 5 | 137 | 0.42 | 0.75 | 28 | empty |
Interfaces
1 interface between chains.
- B–A · 504 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 6UIQ · Crystal structure of wild-type human phosphoglucomutase 1 in complex with… · the same entry in another collection · chain B against B, TM-score 1.00
- P36871 · AlphaFold monomer V2.0 prediction for phosphoglucomutase-1 (P36871) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 6UIQ · PDBe 6UIQ · UniProt P36871
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