Research workbench
The C145A mutant of the amidase from nesterenkonia sp. AN1 in complex with butyramide
Analyse The C145A mutant of the amidase from nesterenkonia sp. AN1 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4IZS
- Type
- protein
- Length
- 261 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
- BMD
- Pockets
- 2 · best druggability 0.38
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amidase (EC 3.5.1.4) | protein | 261 | 35% helix, 26% 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 | 60 | 0.38 | 0.79 | 22 | BMD |
| 2 | 55 | 0.27 | 0.74 | 11 | empty |
Compared structures
- 4IZS · The C145A mutant of the amidase from Nesterenkonia sp. AN1 in complex with butyramide · 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 4IZS · PDBe 4IZS · UniProt D0VWZ1
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