MolNFT v1 · #95750 · protein
The E41Q mutant of the amidase from nesterenkonia sp. AN1 showing the result of michael addition of acrylamide at the active site cysteine
4IZU: “The E41Q mutant of the amidase from nesterenkonia sp. AN1 showing the result of michael addition of…”. X-ray diffraction, 2 ligands (ROP, 1HC), 1 pocket (best druggability 0.37). MolNFT v1 #95750 on GenesisL1: 3D structure, binding…
- PDB
- 4IZU
- Type
- protein
- Length
- 254 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
- ROP, 1HC
- Pockets
- 1 · best druggability 0.37
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amidase (EC 3.5.1.4) | protein | 254 | 35% helix, 28% strand | D0VWZ1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 57 | 0.37 | 0.79 | 19 | ROP |
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 4IZU · The E41Q mutant of the amidase from Nesterenkonia sp. AN1 showing the result of Michael… · 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 4IZU · PDBe 4IZU · UniProt D0VWZ1
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