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Zinc in PDB 1e6x: Myrosinase From Sinapis Alba with A Bound Transition State Analogue,D- Glucono-1,5-Lactone

Enzymatic activity of Myrosinase From Sinapis Alba with A Bound Transition State Analogue,D- Glucono-1,5-Lactone

All present enzymatic activity of Myrosinase From Sinapis Alba with A Bound Transition State Analogue,D- Glucono-1,5-Lactone:
3.2.3.1;

Protein crystallography data

The structure of Myrosinase From Sinapis Alba with A Bound Transition State Analogue,D- Glucono-1,5-Lactone, PDB code: 1e6x 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 / 1.60
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 (%) 13.8 / 17.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Myrosinase From Sinapis Alba with A Bound Transition State Analogue,D- Glucono-1,5-Lactone (pdb code 1e6x). 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 Myrosinase From Sinapis Alba with A Bound Transition State Analogue,D- Glucono-1,5-Lactone, PDB code: 1e6x:

Zinc binding site 1 out of 1 in 1e6x

Go back to Zinc Binding Sites List in 1e6x
Zinc binding site 1 out of 1 in the Myrosinase From Sinapis Alba with A Bound Transition State Analogue,D- Glucono-1,5-Lactone


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Myrosinase From Sinapis Alba with A Bound Transition State Analogue,D- Glucono-1,5-Lactone within 5.0Å range:
probe atom residue distance (Å) B Occ
M:Zn1502

b:13.6
occ:0.50
 NE2 M:HIS56 2.1 12.4 1.0
OD2 M:ASP70 2.2 15.6 1.0
CG M:ASP70 2.8 16.8 1.0
OD1 M:ASP70 2.9 15.2 1.0
CE1 M:HIS56 3.1 13.1 1.0
CD2 M:HIS56 3.1 13.1 1.0
O M:HOH2138 3.6 25.4 1.0
CB M:ASP70 4.1 14.0 1.0
ND1 M:HIS56 4.2 12.3 1.0
CG M:HIS56 4.2 12.4 1.0
ND2 M:ASN68 4.5 16.8 1.0
OD1 M:ASN68 4.8 14.0 1.0
O M:HOH2092 4.8 35.0 1.0
CG M:ASN68 4.9 15.6 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: Wed Dec 16 02:47:59 2020

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