› 1w9d

X-ray diffraction
1.6Å resolution

S. alba myrosinase in complex with S-ethyl phenylacetothiohydroximate- O-sulfate

Released:
DOI: 10.2210/pdb1w9d/pdb
PDB entry 1w9d coloured by chain, front view.
PDB entry 1w9d coloured by chain, side view.
PDB entry 1w9d coloured by chain, top view.
Source organism: Sinapis alba
Primary publication:
The glucosinolate-myrosinase system. New insights into enzyme-substrate interactions by use of simplified inhibitors.
Bourderioux A, Lefoix M, Gueyrard D, Tatibouét A, Cottaz S, Arzt S, Burmeister WP, Rollin P
Org Biomol Chem 3 1872-9 (2005)
PMID: 15889170

Function and Biology Details

Reaction catalysed: 
A thioglucoside + H(2)O = a sugar + a thiol
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151568 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Myrosinase MA1 Chain: M
Molecule details ›
Chain: M
Length: 501 amino acids
Theoretical weight: 57.08 KDa
Source organism: Sinapis alba
UniProt:
  • Canonical: P29736 (Residues: 1-501; Coverage: 100%)
Sequence domains: Glycosyl hydrolase family 1
Structure domains: Glycosidases

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, XYP, FUC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, XYP, FUC, MAN
Carbohydrate polymer
5 bound ligands:
Ligand NAG 6 x NAG
Ligand SEH 1 x SEH
Ligand ZN 1 x ZN
Ligand SO4 4 x SO4
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: C2221
Unit cell:
a: 135.3Å b: 137.2Å c: 80.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 0.195

Quick links

Citations

1 review citation

Glucosinolate metabolism and its control.
Grubb et al. (2006)
7 other articles

2 mentions without citation

Detection of trans-cis flips and peptide-plane flips in protein structures.
Touw et al. (2015)
1 more