MolNFT v1 · #21508 · protein
K236L mutant of hydroxynitrile lyase from hevea brasiliensis in complex with acetonecyanohydrin
1SCQ · (S)-acetone-cyanohydrin lyase: “K236L mutant of hydroxynitrile lyase from hevea brasiliensis in complex with acetonecyanohydrin”. X-ray diffraction, 2 ligands (CNH, SO4). MolNFT v1 #21508 on GenesisL1: 3D structure, binding sites…
- 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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