Research workbench
The crystal structure of beta-phosphoglucomutase from bacillus subtilis
Analyse The crystal structure of beta-phosphoglucomutase from bacillus subtilis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3NAS
- Type
- protein
- Length
- 412 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-phosphoglucomutase
- EC
- 5.4.2.6
- UniProt
- O06995
- Pockets
- 6 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 53% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-phosphoglucomutase (EC 5.4.2.6) | protein | 207 | 53% helix, 11% strand | O06995 |
| B | Beta-phosphoglucomutase (EC 5.4.2.6) | protein | 205 | 53% helix, 11% strand | O06995 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 324 | 0.66 | 0.81 | 51 | empty |
| 2 | 73 | 0.49 | 0.84 | 17 | empty |
| 3 | 72 | 0.46 | 0.82 | 18 | empty |
| 4 | 129 | 0.38 | 0.74 | 22 | empty |
| 5 | 61 | 0.34 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 508 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 11 modified, 1 disulfide (engineered, disulfide).
Compared structures
- 3NAS · The crystal structure of beta-phosphoglucomutase from Bacillus subtilis · the same entry in another collection · chain A against A, TM-score 1.00
- O06995 · AlphaFold monomer V2.0 prediction for beta-phosphoglucomutase (O06995) · a predicted model of the same protein · chain B against A, TM-score 0.85
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 O06995
- Elsewhere: RCSB PDB 3NAS · PDBe 3NAS · UniProt O06995
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