Research workbench
Mycobacterium tuberculosis eis protein initiates modulation of host immune responses by acetylation of DUSP16/MKP-7
Analyse Mycobacterium tuberculosis eis protein initiates modulation of host immune… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SXN
- Type
- protein
- Length
- 2,412 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enhanced intracellular survival protein
- UniProt
- A0QY29
- Ligands
- COA
- Pockets
- 20 · best druggability 0.89
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Enhanced intracellular survival protein | protein | 402 | 30% helix, 31% strand | A0QY29 |
Ligands and binding sites
- COA · Coenzyme A · ligand · 6 copies · chains A, F, B, D, C, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 967 | 0.89 | 0.91 | 122 | empty |
| 2 | 1095 | 0.87 | 0.88 | 127 | empty |
| 3 | 1183 | 0.86 | 0.87 | 143 | empty |
| 4 | 912 | 0.84 | 0.85 | 103 | COA |
| 5 | 878 | 0.83 | 0.85 | 105 | COA |
Interfaces
12 interfaces between chains.
- A–B · 1796 Ų buried · 24 hydrogen bonds · protein-protein
- C–D · 1746 Ų buried · 26 hydrogen bonds · protein-protein
- E–F · 1729 Ų buried · 20 hydrogen bonds · protein-protein
- A–F · 929 Ų buried · 16 hydrogen bonds · protein-protein
- B–D · 913 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 3SXN · Mycobacterium tuberculosis Eis protein initiates modulation of host immune responses by… · 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 A0QY29
- Elsewhere: RCSB PDB 3SXN · PDBe 3SXN · UniProt A0QY29
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