Research workbench
Structure of the CFP10-ESAT6 complex from mycobacterium tuberculosis
Analyse Structure of the CFP10-ESAT6 complex 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
- 3FAV
- Type
- protein
- Length
- 314 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Esat-6-like protein esxb; 6 kda early secretory antigenic target
- UniProt
- P0A566, P0A564
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.43
Structure
x-ray diffraction · 4 distinct chains · 91% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Esat-6-like protein esxb | protein | 74 | 88% helix, 0% strand | P0A566 |
| B | 6 kda early secretory antigenic target | protein | 72 | 89% helix, 0% strand | P0A564 |
| C | Esat-6-like protein esxb | protein | 90 | 96% helix, 0% strand | P0A566 |
| D | 6 kda early secretory antigenic target | protein | 78 | 90% helix, 0% strand | P0A564 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 102 | 0.43 | 0.78 | 25 | empty |
Interfaces
4 interfaces between chains.
- C–D · 1660 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 1508 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 266 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 93 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3FAV · Structure of the CFP10-ESAT6 complex from 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 P0A566
- Every structure of UniProt P0A564
- Elsewhere: RCSB PDB 3FAV · PDBe 3FAV · UniProt P0A566 · UniProt P0A564
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.