Research workbench
Hydroxynitrile lyase from hevea brasiliensis in complex with the natural substrate acetone cyanohydrin
Analyse Hydroxynitrile lyase from hevea brasiliensis in complex with the natural… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SC9
- 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
- Pockets
- 1 · best druggability 0.34
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | (S)-acetone-cyanohydrin lyase (EC 4.1.2.39) | protein | 256 | 40% helix, 18% strand | P52704 |
Ligands and binding sites
- CNH · 2-hydroxy-2-methylpropanenitrile · ligand · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
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 | 53 | 0.34 | 0.78 | 12 | empty |
Compared structures
- 1SC9 · Hydroxynitrile Lyase from Hevea brasiliensis in complex with the natural substrate… · 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 1SC9 · PDBe 1SC9 · UniProt P52704
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