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Hnl from hevea brasiliensis to atomic resolution

Analyse Hnl from hevea brasiliensis to atomic resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3C6Y
Type: protein
Length: 256 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hydroxynitrilase
EC: 4.1.2.37
UniProt: P52704
Ligands: ACN, SO4

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hydroxynitrilase (EC 4.1.2.37)	protein	256	41% helix, 20% strand	P52704

Ligands and binding sites

ACN · Acetone · ligand · chains A
SO4 · Sulfate ion · ion · 4 copies · chains A
BME · Beta-mercaptoethanol · additive · chains A
PEG · Di(hydroxyethyl)ether · additive · chains A

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

Modifications

Observed in the structure: 1 covalent (additive adduct).

Compared structures

3C6Y · HNL from Hevea brasiliensis to atomic resolution · 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 3C6Y · PDBe 3C6Y · UniProt P52704

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