Research workbench
Crystal structure of the bacterial proteasome activator bpa of mycobacterium tuberculosis (space group P6322, semet)
Analyse Crystal structure of the bacterial proteasome activator bpa of mycobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LFP
- Type
- protein
- Length
- 432 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bacterial proteasome activator
- UniProt
- P9WKX3
- Pockets
- 4 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Bacterial proteasome activator | protein | 108 | 79% helix, 0% strand | P9WKX3 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 338 | 0.58 | 0.76 | 51 | empty |
| 2 | 122 | 0.41 | 0.75 | 23 | empty |
| 3 | 55 | 0.40 | 0.81 | 10 | empty |
| 4 | 54 | 0.35 | 0.78 | 12 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1127 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 1125 Ų buried · 16 hydrogen bonds · protein-protein
- C–D · 1104 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 5LFP · Crystal Structure of the Bacterial Proteasome Activator Bpa of Mycobacterium tuberculosis… · the same entry in another collection · chain D against D, TM-score 1.00
- P9WKX3 · AlphaFold monomer V2.0 prediction for bacterial proteasome activator (P9WKX3) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P9WKX3
- Elsewhere: RCSB PDB 5LFP · PDBe 5LFP · UniProt P9WKX3
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