Research workbench
Crystal structure of the G121R mutant of human phosphoglucomutase 1
Analyse Crystal structure of the G121R 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
- 5F9C
- Type
- protein
- Length
- 1,086 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
- MG, SO4
- Pockets
- 8 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoglucomutase-1 (EC 5.4.2.2) | protein | 550 | 35% helix, 25% strand | P36871 |
| B | Phosphoglucomutase-1 (EC 5.4.2.2) | protein | 536 | 36% helix, 24% strand | P36871 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 9 copies · chains A, B
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 562 | 0.70 | 0.79 | 57 | SO4 |
| 2 | 507 | 0.64 | 0.76 | 57 | SO4 |
| 3 | 546 | 0.64 | 0.76 | 72 | SO4, MG |
| 4 | 127 | 0.43 | 0.76 | 24 | GOL |
| 5 | 89 | 0.35 | 0.75 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 534 Ų buried · 6 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 5F9C · PDBe 5F9C · UniProt P36871
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