Research workbench
The E142L mutant of the amidase from geobacillus pallidus showing the result of michael addition of acrylamide at the active site cysteine
Analyse The E142L mutant of the amidase from geobacillus pallidus 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
- 4GYL
- Type
- protein
- Length
- 340 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aliphatic amidase
- EC
- 3.5.1.4
- UniProt
- Q9L543
- Ligands
- ROP, CL
- Pockets
- 1 · best druggability 0.27
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aliphatic amidase (EC 3.5.1.4) | protein | 340 | 33% helix, 24% strand | Q9L543 |
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 | 0.27 | 0.73 | 16 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 4GYL · The E142L mutant of the amidase from Geobacillus pallidus showing the result of Michael… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9L543 · AlphaFold monomer V2.0 prediction for aliphatic amidase (Q9L543) · a predicted model of the same protein · 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 Q9L543
- Elsewhere: RCSB PDB 4GYL · PDBe 4GYL · UniProt Q9L543
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