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Crystal structure of a bacterial phosphoglucomutase, an enzyme important in the virulence of multiple human pathogens
Analyse Crystal structure of a bacterial phosphoglucomutase, an enzyme important in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OLP
- Type
- protein
- Length
- 1,086 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoglucomutase
- EC
- 5.4.2.2
- UniProt
- Q8ZQW9
- Ligands
- MG, PO4
- Pockets
- 6 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoglucomutase (EC 5.4.2.2) | protein | 543 | 38% helix, 21% strand | Q8ZQW9 |
| B | Phosphoglucomutase (EC 5.4.2.2) | protein | 543 | 38% helix, 21% strand | Q8ZQW9 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 738 | 0.67 | 0.75 | 70 | PO4 |
| 2 | 448 | 0.64 | 0.77 | 65 | empty |
| 3 | 436 | 0.59 | 0.75 | 47 | PO4 |
| 4 | 96 | 0.40 | 0.76 | 21 | empty |
| 5 | 71 | 0.37 | 0.77 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1110 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- 3OLP · Crystal structure of a bacterial phosphoglucomutase, an enzyme important in the virulence… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q8ZQW9
- Elsewhere: RCSB PDB 3OLP · PDBe 3OLP · UniProt Q8ZQW9
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