Research workbench
Human N-acetyltransferase 1 F125S mutant
Analyse Human N-acetyltransferase 1 F125S mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IJA
- Type
- protein
- Length
- 292 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arylamine N-acetyltransferase 1
- EC
- 2.3.1.5
- UniProt
- P18440
- Ligands
- ACM, NA, UNX
- Pockets
- 1 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arylamine N-acetyltransferase 1 (EC 2.3.1.5) | protein | 292 | 29% helix, 29% strand | P18440 |
Ligands and binding sites
- ACM · Acetamide · ligand · chains A
- NA · Sodium ion · metal · chains A
- UNX · Unknown atom or ion · ion · 7 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 267 | 0.71 | 0.85 | 34 | ACM |
Modifications
Observed in the structure: 5 modified, 1 covalent (engineered, covalent ligand).
Compared structures
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 P18440
- Elsewhere: RCSB PDB 2IJA · PDBe 2IJA · UniProt P18440
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