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Crystal structure of espr transcription factor from mycobacterium tuberculosis
Analyse Crystal structure of espr transcription factor from mycobacterium tuberculosis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QF3
- Type
- protein
- Length
- 780 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Esx-1 secretion-associated regulator espr
- UniProt
- P96228
- Ligands
- MLT, LMR
- Pockets
- 8 · best druggability 0.76
Structure
x-ray diffraction · 4 distinct chains · 68% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, E | Esx-1 secretion-associated regulator espr | protein | 131 | 69% helix, 0% strand | P96228 |
| D | Esx-1 secretion-associated regulator espr | protein | 128 | 68% helix, 0% strand | P96228 |
| C | Esx-1 secretion-associated regulator espr | protein | 129 | 68% helix, 0% strand | P96228 |
| F | Esx-1 secretion-associated regulator espr | protein | 130 | 66% helix, 0% strand | P96228 |
Ligands and binding sites
- MLT · D-malate · ligand · 2 copies · chains B, C, E, F
- LMR · (2S)-2-hydroxybutanedioic acid · ligand · chains A, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 222 | 0.76 | 0.90 | 30 | MLT |
| 2 | 128 | 0.75 | 0.94 | 26 | LMR |
| 3 | 196 | 0.75 | 0.91 | 33 | MLT |
| 4 | 486 | 0.62 | 0.76 | 50 | empty |
| 5 | 395 | 0.58 | 0.75 | 53 | empty |
Interfaces
6 interfaces between chains.
- B–C · 2471 Ų buried · 21 hydrogen bonds · protein-protein
- A–D · 2377 Ų buried · 21 hydrogen bonds · protein-protein
- E–F · 2307 Ų buried · 20 hydrogen bonds · protein-protein
- D–B · 562 Ų buried · 9 hydrogen bonds · protein-protein
- B–E · 358 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 3QF3 · Crystal structure of EspR transcription factor from mycobacterium tuberculosis · the same entry in another collection · chain D against D, 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 3QF3 · PDBe 3QF3 · UniProt P96228
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