MolNFT v1 · #95749 · protein
The E41Q mutant of the amidase from nesterenkonia sp. AN1 showing covalent addition of the acetamide moiety of fluoroacetamide at the active site cysteine
4IZT: “The E41Q mutant of the amidase from nesterenkonia sp. AN1 showing covalent addition of the acetamide moiety…”. X-ray diffraction, 2 ligands (FTM, ACM), 2 pockets (best druggability 0.42). MolNFT v1 #95749 on GenesisL1: 3D structure…
- PDB
- 4IZT
- Type
- protein
- Length
- 263 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amidase
- EC
- 3.5.1.4
- UniProt
- D0VWZ1
- Ligands
- FTM, ACM
- Pockets
- 2 · best druggability 0.42
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amidase (EC 3.5.1.4) | protein | 263 | 33% helix, 28% strand | D0VWZ1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 90 | 0.42 | 0.78 | 22 | ACM, FTM |
| 2 | 61 | 0.28 | 0.74 | 13 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 4IZT · The E41Q mutant of the amidase from Nesterenkonia sp. AN1 showing covalent addition of… · 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 D0VWZ1
- Elsewhere: RCSB PDB 4IZT · PDBe 4IZT · UniProt D0VWZ1
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