MolNFT v1 · #21494 · protein

Hydroxynitrile lyase from hevea brasiliensis in complex with the natural substrate acetone cyanohydrin

1SC9 · (S)-acetone-cyanohydrin lyase: “Hydroxynitrile lyase from hevea brasiliensis in complex with the natural substrate acetone cyanohydrin”. X-ray diffraction, 2 ligands (CNH, SO4), 1 pocket (best druggability 0.34). MolNFT v1 #21494 on…

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.

Pocket	Volume (Å³)	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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