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Hydroxynitrile lyase complexed with histidine

Analyse Hydroxynitrile lyase complexed with histidine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1YAS
Type: protein
Length: 256 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hydroxynitrile lyase
EC: 4.1.2.39
UniProt: P52704
Ligands: HIS, SO4
Pockets: 2 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hydroxynitrile lyase (EC 4.1.2.39)	protein	256	41% helix, 19% strand	P52704

Ligands and binding sites

HIS · Histidine · ligand · chains A
SO4 · Sulfate ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	66	0.75	0.98	20	HIS
2	57	0.33	0.77	13	empty

Compared structures

1YAS · Hydroxynitrile lyase complexed with histidine · 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 1YAS · PDBe 1YAS · UniProt P52704

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