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

Enzymatic activity of 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;

Protein crystallography data

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

Zinc Binding Sites:

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 1e73

Go back to Zinc Binding Sites List in 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

Reference:

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
Page generated: Fri Sep 25 21:23:22 2020
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