Zinc in PDB 1w9d: S. Alba Myrosinase in Complex with S-Ethyl Phenylacetothiohydroximate- O-Sulfate

All present enzymatic activity of S. Alba Myrosinase in Complex with S-Ethyl Phenylacetothiohydroximate- O-Sulfate:
3.2.3.1;

The structure of S. Alba Myrosinase in Complex with S-Ethyl Phenylacetothiohydroximate- O-Sulfate, PDB code: 1w9d was solved by A.Bourderioux, M.Lefoix, D.Gueyrard, A.Tatibouet, S.Cottaz, S.Arzt, W.P.Burmeister, P.Rollin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.00 / 1.60
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	135.300, 137.200, 80.600, 90.00, 90.00, 90.00
R / Rfree (%)	18.9 / 19.5

The binding sites of Zinc atom in the S. Alba Myrosinase in Complex with S-Ethyl Phenylacetothiohydroximate- O-Sulfate (pdb code 1w9d). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the S. Alba Myrosinase in Complex with S-Ethyl Phenylacetothiohydroximate- O-Sulfate, PDB code: 1w9d:

Zinc binding site 1 out of 1 in the S. Alba Myrosinase in Complex with S-Ethyl Phenylacetothiohydroximate- O-Sulfate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of S. Alba Myrosinase in Complex with S-Ethyl Phenylacetothiohydroximate- O-Sulfate within 5.0Å range: probe atom residue distance (Å) B Occ M:Zn1502 b:8.1 occ:0.50 NE2 M:HIS56 2.0 6.3 1.0 OD2 M:ASP70 2.1 8.2 1.0 CG M:ASP70 2.8 9.4 1.0 OD1 M:ASP70 2.9 8.6 1.0 CE1 M:HIS56 3.0 8.2 1.0 CD2 M:HIS56 3.0 8.9 1.0 O M:HOH2141 3.7 22.1 1.0 ND1 M:HIS56 4.1 7.7 1.0 CG M:HIS56 4.2 8.2 1.0 CB M:ASP70 4.2 9.0 1.0 ND2 M:ASN68 4.6 11.4 1.0 O M:HOH2092 4.6 29.3 1.0 OD1 M:ASN68 4.8 9.5 1.0 CG M:ASN68 5.0 10.3 1.0

A.Bourderioux, M.Lefoix, D.Gueyrard, A.Tatibouet, S.Cottaz, S.Arzt, W.P.Burmeister, P.Rollin. The Glucosinolate-Myrosinase System. New Insights Into Enzyme-Substrate Interactions By Use of Simplified Inhibitors Org.Biomol.Chem. V. 3 1872 2005.
ISSN: ISSN 1477-0520
PubMed: 15889170
DOI: 10.1039/B502990B