Research workbench
Crystal structure of eis from mycobacterium tuberculosis in complex with inhibitor SGT366
Analyse Crystal structure of eis from mycobacterium tuberculosis in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VUR
- Type
- protein
- Length
- 396 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-acetyltransferase eis
- EC
- 2.3.1.-
- UniProt
- P9WFK7
- Ligands
- ROG, NA, SO4, 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 | N-acetyltransferase eis (EC 2.3.1.-) | protein | 396 | 31% helix, 31% strand | P9WFK7 |
Ligands and binding sites
- ROG · 2-({[(3S)-1-methylpiperidin-3-yl]methyl}sulfanyl)-5,6, 7,8-tetrahydro[1]benzothieno[2,3-d]pyrimidin-4-amine · ligand · chains A
- NA · Sodium ion · metal · 2 copies · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A
- CL · Chloride ion · ion · 3 copies · chains A
- GOL · Glycerol · additive · 3 copies · chains A
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · 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 | 1060 | 0.78 | 0.80 | 94 | ROG, GOL, PEG, NA, SO4, CL |
| 2 | 62 | 0.32 | 0.76 | 14 | PEG |
| 3 | 53 | 0.29 | 0.76 | 18 | SO4 |
Compared structures
- 6VUR · Crystal structure of Eis from Mycobacterium tuberculosis in complex with inhibitor SGT366 · 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 6VUR · PDBe 6VUR · UniProt P9WFK7
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