Research workbench
Crystal structure of mycobacterium tuberculosis bfrb
Analyse Crystal structure of mycobacterium tuberculosis bfrb in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QD8
- Type
- protein
- Length
- 3,898 residues
- Chains
- 24
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable bacterioferritin bfrb
- UniProt
- P96237
- Pockets
- 20 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 74% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable bacterioferritin bfrb | protein | 172 | 72% helix, 1% strand | P96237 |
| B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X | Probable bacterioferritin bfrb | protein | 162 | 76% helix, 1% strand | P96237 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 64 | 0.75 | 0.99 | 14 | empty |
| 2 | 925 | 0.75 | 0.78 | 90 | empty |
| 3 | 66 | 0.75 | 0.99 | 15 | empty |
| 4 | 70 | 0.75 | 0.98 | 14 | empty |
| 5 | 69 | 0.74 | 0.98 | 15 | empty |
Interfaces
60 interfaces between chains.
- Q–V · 1168 Ų buried · 11 hydrogen bonds · protein-protein
- R–U · 1164 Ų buried · 11 hydrogen bonds · protein-protein
- J–M · 1163 Ų buried · 11 hydrogen bonds · protein-protein
- O–P · 1162 Ų buried · 11 hydrogen bonds · protein-protein
- B–E · 1160 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 3QD8 · Crystal structure of Mycobacterium tuberculosis BfrB · 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 P96237
- Elsewhere: RCSB PDB 3QD8 · PDBe 3QD8 · UniProt P96237
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