Research workbench

K236L mutant of hydroxynitrile lyase from hevea brasiliensis

Analyse K236L mutant of hydroxynitrile lyase from hevea brasiliensis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1SCI
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: SO4

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	(S)-acetone-cyanohydrin lyase (EC 4.1.2.39)	protein	256	40% helix, 20% strand	P52704

Ligands and binding sites

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

1SCI · K236L mutant of hydroxynitrile lyase from Hevea brasiliensis · 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 1SCI · PDBe 1SCI · UniProt P52704

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