Research workbench
A C145S mutant of nesterenkonia AN1 amidase from the nitrilase superfamily
Analyse A C145S mutant of nesterenkonia AN1 amidase from the nitrilase superfamily in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NZ5
- Type
- protein
- Length
- 259 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amidase
- EC
- 3.5.1.4
- UniProt
- D0VWZ1
- Pockets
- 2 · best druggability 0.41
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amidase (EC 3.5.1.4) | protein | 259 | 35% helix, 27% strand | D0VWZ1 |
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 | 78 | 0.41 | 0.79 | 21 | empty |
| 2 | 55 | 0.27 | 0.74 | 11 | empty |
Compared structures
- 5NZ5 · A C145S mutant of Nesterenkonia AN1 amidase from the nitrilase superfamily · 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 5NZ5 · PDBe 5NZ5 · UniProt D0VWZ1
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