Zinc in PDB 1e73: 2-F-Glucosylated Myrosinase From Sinapis Alba with Bound L-Ascorbate

All present enzymatic activity of 2-F-Glucosylated Myrosinase From Sinapis Alba with Bound L-Ascorbate:
3.2.1.147;

The structure of 2-F-Glucosylated Myrosinase From Sinapis Alba with Bound L-Ascorbate, PDB code: 1e73 was solved by W.P.Burmeister, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.50
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 (%)	13.4 / 16.7

The binding sites of Zinc atom in the 2-F-Glucosylated Myrosinase From Sinapis Alba with Bound L-Ascorbate (pdb code 1e73). 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 2-F-Glucosylated Myrosinase From Sinapis Alba with Bound L-Ascorbate, PDB code: 1e73:

Zinc binding site 1 out of 1 in the 2-F-Glucosylated Myrosinase From Sinapis Alba with Bound L-Ascorbate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of 2-F-Glucosylated Myrosinase From Sinapis Alba with Bound L-Ascorbate within 5.0Å range: probe atom residue distance (Å) B Occ M:Zn1515 b:11.2 occ:0.50 OD2 M:ASP70 2.0 11.4 1.0 NE2 M:HIS56 2.1 10.1 1.0 CG M:ASP70 2.7 11.8 1.0 OD1 M:ASP70 3.0 11.5 1.0 CE1 M:HIS56 3.0 11.8 1.0 CD2 M:HIS56 3.1 12.3 1.0 O M:HOH2134 3.7 20.7 1.0 CB M:ASP70 4.1 13.1 1.0 ND1 M:HIS56 4.2 11.8 1.0 CG M:HIS56 4.2 11.9 1.0 ND2 M:ASN68 4.4 14.3 1.0 OD1 M:ASN68 4.8 14.1 1.0 O M:HOH2091 4.8 33.9 1.0 CG M:ASN68 4.9 14.0 1.0

W.P.Burmeister, S.Cottaz, P.Rollin, A.Vasella, B.Henrissat. High Resolution X-Ray Crystallography Shows That Ascorbate Is A Cofactor For Myrosinase and Substitutes For the Function of the Catalytic Base J.Biol.Chem. V. 275 39385 2000.
ISSN: ISSN 0021-9258
PubMed: 10978344
DOI: 10.1074/JBC.M006796200