Research workbench
Crystal structure of a key regulator of virulence in mycobacterium tuberculosis
Analyse Crystal structure of a key regulator of virulence in mycobacterium tuberculosis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3R1F
- Type
- protein
- Length
- 2,191 residues
- Chains
- 18
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Esx-1 secretion-associated regulator espr
- UniProt
- P96228
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · 11 distinct chains · 65% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Esx-1 secretion-associated regulator espr | protein | 123 | 67% helix, 0% strand | P96228 |
| B, D, F, H, J, N | Esx-1 secretion-associated regulator espr | protein | 130 | 65% helix, 0% strand | P96228 |
| C, G | Esx-1 secretion-associated regulator espr | protein | 123 | 68% helix, 0% strand | P96228 |
| E | Esx-1 secretion-associated regulator espr | protein | 125 | 66% helix, 0% strand | P96228 |
| I, K | Esx-1 secretion-associated regulator espr | protein | 124 | 66% helix, 0% strand | P96228 |
| L | Esx-1 secretion-associated regulator espr | protein | 129 | 67% helix, 0% strand | P96228 |
| M | Esx-1 secretion-associated regulator espr | protein | 119 | 66% helix, 0% strand | P96228 |
| O | Esx-1 secretion-associated regulator espr | protein | 90 | 58% helix, 0% strand | P96228 |
| P | Esx-1 secretion-associated regulator espr | protein | 92 | 64% helix, 0% strand | P96228 |
| Q | Esx-1 secretion-associated regulator espr | protein | 116 | 66% helix, 0% strand | P96228 |
| R | Esx-1 secretion-associated regulator espr | protein | 123 | 61% helix, 0% strand | P96228 |
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 226 | 0.77 | 0.91 | 33 | empty |
| 2 | 190 | 0.77 | 0.92 | 33 | empty |
| 3 | 221 | 0.77 | 0.91 | 32 | empty |
| 4 | 223 | 0.76 | 0.91 | 30 | empty |
| 5 | 202 | 0.76 | 0.91 | 32 | empty |
Interfaces
10 interfaces between chains.
- E–F · 2400 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 2399 Ų buried · 16 hydrogen bonds · protein-protein
- C–D · 2362 Ų buried · 22 hydrogen bonds · protein-protein
- K–L · 2345 Ų buried · 15 hydrogen bonds · protein-protein
- G–H · 2344 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 53 modified (engineered).
Compared structures
- 3R1F · Crystal structure of a key regulator of virulence in Mycobacterium tuberculosis · 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 P96228
- Elsewhere: RCSB PDB 3R1F · PDBe 3R1F · UniProt P96228
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.