Research workbench
Mycobacterium tuberculosis ahpc
Analyse Mycobacterium tuberculosis ahpc in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BMX
- Type
- protein
- Length
- 516 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alkyl hydroperoxidase C
- EC
- 1.11.1.15
- UniProt
- Q7BHK8
- Pockets
- 4 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Alkyl hydroperoxidase C (EC 1.11.1.15) | protein | 169 | 31% helix, 26% strand | Q7BHK8 |
| B | Alkyl hydroperoxidase C (EC 1.11.1.15) | protein | 178 | 30% helix, 25% strand | Q7BHK8 |
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 121 | 0.78 | 0.96 | 31 | empty |
| 2 | 88 | 0.73 | 0.95 | 22 | empty |
| 3 | 98 | 0.67 | 0.91 | 22 | empty |
| 4 | 84 | 0.63 | 0.90 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 1148 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified, 1 disulfide (engineered, disulfide).
Compared structures
- 2BMX · Mycobacterium tuberculosis AhpC · 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 Q7BHK8
- Elsewhere: RCSB PDB 2BMX · PDBe 2BMX · UniProt Q7BHK8
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