Research workbench
The E41Q mutant of the amidase from nesterenkonia sp. AN1 showing the result of michael addition of acrylamide at the active site cysteine
Analyse The E41Q mutant of the amidase from nesterenkonia sp. AN1 showing the result of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- 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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