Research workbench
K236L mutant of hydroxynitrile lyase from hevea brasiliensis in complex with acetonecyanohydrin
Analyse K236L mutant of hydroxynitrile lyase from hevea brasiliensis 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
- 1SCQ
- Type
- protein
- Length
- 256 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- (S)-acetone-cyanohydrin lyase
- EC
- 4.1.2.39
- UniProt
- P52704
- Ligands
- CNH, SO4
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | (S)-acetone-cyanohydrin lyase (EC 4.1.2.39) | protein | 256 | 39% helix, 19% strand | P52704 |
Ligands and binding sites
- CNH · 2-hydroxy-2-methylpropanenitrile · ligand · chains A
- SO4 · Sulfate ion · ion · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1SCQ · K236L mutant of hydroxynitrile lyase from Hevea brasiliensis in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- P52704 · AlphaFold monomer V2.0 prediction for (S)-hydroxynitrile lyase (P52704) · 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 P52704
- Elsewhere: RCSB PDB 1SCQ · PDBe 1SCQ · UniProt P52704
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