MolNFT v1 · #125662 · protein
Crystal structure of the bacterial proteasome activator bpa of mycobacterium tuberculosis (space group P3)
5LFQ: “Crystal structure of the bacterial proteasome activator bpa of mycobacterium tuberculosis (space group P3)”. X-ray diffraction, 20 pockets (best druggability 0.58). MolNFT v1 #125662 on GenesisL1: 3D structure, binding sites and…
- PDB
- 5LFQ
- Type
- protein
- Length
- 1,808 residues
- Chains
- 16
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bacterial proteasome activator
- UniProt
- P9WKX3
- Pockets
- 20 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 75% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P | Bacterial proteasome activator | protein | 113 | 75% helix, 2% strand | P9WKX3 |
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 254 | 0.58 | 0.78 | 36 | empty |
| 2 | 279 | 0.57 | 0.77 | 26 | empty |
| 3 | 224 | 0.56 | 0.78 | 32 | empty |
| 4 | 219 | 0.55 | 0.78 | 25 | empty |
| 5 | 211 | 0.54 | 0.78 | 21 | empty |
Interfaces
27 interfaces between chains.
- G–H · 1153 Ų buried · 16 hydrogen bonds · protein-protein
- O–P · 1153 Ų buried · 13 hydrogen bonds · protein-protein
- I–J · 1150 Ų buried · 12 hydrogen bonds · protein-protein
- B–G · 1140 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 1136 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 48 modified (engineered).
Compared structures
- 5LFQ · Crystal Structure of the Bacterial Proteasome Activator Bpa of Mycobacterium tuberculosis… · the same entry in another collection · chain I against I, 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 P9WKX3
- Elsewhere: RCSB PDB 5LFQ · PDBe 5LFQ · UniProt P9WKX3
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