Research workbench
Crystal structure of phosphoglucosamine mutase from B. anthracis
Analyse Crystal structure of phosphoglucosamine mutase from B. anthracis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PDK
- Type
- protein
- Length
- 889 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoglucosamine mutase
- EC
- 5.4.2.10
- UniProt
- Q81VN7
- Ligands
- PO4
- Pockets
- 9 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoglucosamine mutase (EC 5.4.2.10) | protein | 445 | 40% helix, 21% strand | Q81VN7 |
| B | Phosphoglucosamine mutase (EC 5.4.2.10) | protein | 444 | 39% helix, 21% strand | Q81VN7 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 8 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 256 | 0.73 | 0.87 | 35 | PO4 |
| 2 | 472 | 0.70 | 0.80 | 49 | PO4 |
| 3 | 453 | 0.68 | 0.80 | 47 | PO4 |
| 4 | 126 | 0.55 | 0.83 | 24 | empty |
| 5 | 55 | 0.48 | 0.85 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1234 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 3PDK · crystal structure of phosphoglucosamine mutase from B. anthracis · the same entry in another collection · chain A against A, TM-score 1.00
- Q81VN7 · AlphaFold monomer V2.0 prediction for phosphoglucosamine mutase (Q81VN7) · a predicted model of the same protein · chain A 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 Q81VN7
- Elsewhere: RCSB PDB 3PDK · PDBe 3PDK · UniProt Q81VN7
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