Research workbench
Hydroxynitrile lyase from hevea brasiliensis complexed with rhodanide
Analyse Hydroxynitrile lyase from hevea brasiliensis complexed with rhodanide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YAS
- Type
- protein
- Length
- 256 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (hydroxynitrile lyase)
- EC
- 4.1.2.39
- UniProt
- P52704
- Ligands
- SO4, SCN
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (hydroxynitrile lyase) (EC 4.1.2.39) | protein | 256 | 41% helix, 18% strand | P52704 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2YAS · Hydroxynitrile lyase from hevea brasiliensis complexed with rhodanide · 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 2YAS · PDBe 2YAS · UniProt P52704
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.