Research workbench
Arylamine N-acetyltransferase (nat) from salmonella typhimurium
Analyse Arylamine N-acetyltransferase (nat) from salmonella typhimurium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1E2T
- Type
- protein
- Length
- 2,192 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-hydroxyarylamine O-acetyltransferase
- EC
- 2.3.1.118
- UniProt
- Q00267
- Pockets
- 20 · best druggability 0.88
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | N-hydroxyarylamine O-acetyltransferase (EC 2.3.1.118) | protein | 274 | 31% helix, 25% strand | Q00267 |
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1072 | 0.88 | 0.89 | 114 | empty |
| 2 | 1058 | 0.88 | 0.89 | 117 | empty |
| 3 | 866 | 0.74 | 0.78 | 71 | empty |
| 4 | 192 | 0.74 | 0.90 | 27 | empty |
| 5 | 222 | 0.67 | 0.84 | 37 | empty |
Interfaces
15 interfaces between chains.
- B–C · 804 Ų buried · 18 hydrogen bonds · protein-protein
- A–D · 803 Ų buried · 10 hydrogen bonds · protein-protein
- F–H · 788 Ų buried · 17 hydrogen bonds · protein-protein
- E–G · 785 Ų buried · 13 hydrogen bonds · protein-protein
- E–H · 554 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 1E2T · Arylamine N-acetyltransferase (NAT) from Salmonella typhimurium · the same entry in another collection · chain H against H, TM-score 1.00
- Q00267 · AlphaFold monomer V2.0 prediction for arylamine N-acetyltransferase / N-hydroxyarylamine… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q00267
- Elsewhere: RCSB PDB 1E2T · PDBe 1E2T · UniProt Q00267
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