MolNFT v1 · #87587 · protein
The structure of mycobacterium marinum arylamine N-acetyltransferase
4C5P: “The structure of mycobacterium marinum arylamine N-acetyltransferase”. X-ray diffraction, 2 ligands (AZI, SO4), 1 pocket (best druggability 0.62). MolNFT v1 #87587 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4C5P
- Type
- protein
- Length
- 272 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arylamine N-acetyltransferase
- EC
- 2.3.1.5
- UniProt
- B2HIZ6
- Ligands
- AZI, SO4
- Pockets
- 1 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arylamine N-acetyltransferase (EC 2.3.1.5) | protein | 272 | 34% helix, 26% strand | B2HIZ6 |
Ligands and binding sites
- AZI · Azide ion · ion · 2 copies · chains A
- SO4 · Sulfate 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
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 | 376 | 0.62 | 0.77 | 46 | AZI |
Modifications
Observed in the structure: 1 modified (oxidation).
Compared structures
- 4C5P · The structure of mycobacterium marinum arylamine n-acetyltransferase · 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 B2HIZ6
- Elsewhere: RCSB PDB 4C5P · PDBe 4C5P · UniProt B2HIZ6
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