Research workbench
Crystal structure of acetyltransferase eis from mycobacterium tuberculosis in complex with CoA and inhibitor 2K*: 1-(4- fluorophenyl)-2-[2-(4-methylphenyl)-2-OXOETHYL]PYRROLO[1,2-A]PYRAZIN- 2-ium
Analyse Crystal structure of acetyltransferase eis from mycobacterium tuberculosis in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5TVJ
- Type
- protein
- Length
- 396 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enhanced intracellular survival protein
- UniProt
- P9WFK7
- Ligands
- COA, 7LF, CL
- Pockets
- 3 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enhanced intracellular survival protein | protein | 396 | 31% helix, 31% strand | P9WFK7 |
Ligands and binding sites
- COA · Coenzyme A · ligand · chains A
- 7LF · 1-(4-fluorophenyl)-2-[2-(4-methylphenyl)-2-oxoethyl]pyrrolo[1,2-a]pyrazin-2-ium · ligand · chains A
- CL · Chloride ion · ion · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1071 | 0.78 | 0.80 | 94 | COA, 7LF, GOL |
| 2 | 65 | 0.32 | 0.75 | 14 | empty |
| 3 | 52 | 0.30 | 0.76 | 16 | empty |
Compared structures
- 5TVJ · Crystal structure of acetyltransferase Eis from Mycobacterium tuberculosis in complex… · the same entry in another collection · chain A against A, TM-score 1.00
- P9WFK7 · AlphaFold monomer V2.0 prediction for N-acetyltransferase eis (P9WFK7) · a predicted model of the same protein · 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 P9WFK7
- Elsewhere: RCSB PDB 5TVJ · PDBe 5TVJ · UniProt P9WFK7
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