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Zinc in PDB 2vwq: Haloferax Mediterranei Glucose Dehydrogenase in Complex with Nadp and Zn.

Enzymatic activity of Haloferax Mediterranei Glucose Dehydrogenase in Complex with Nadp and Zn.

All present enzymatic activity of Haloferax Mediterranei Glucose Dehydrogenase in Complex with Nadp and Zn.:
1.1.1.47;

Protein crystallography data

The structure of Haloferax Mediterranei Glucose Dehydrogenase in Complex with Nadp and Zn., PDB code: 2vwq was solved by P.J.Baker, K.L.Britton, M.Fisher, J.Esclapez, C.Pire, M.J.Bonete, J.Ferrer, D.W.Rice, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 2.10
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 61.884, 111.113, 152.227, 90.00, 90.00, 90.00
R / Rfree (%) 14.3 / 17.5

Zinc Binding Sites:

The binding sites of Zinc atom in the Haloferax Mediterranei Glucose Dehydrogenase in Complex with Nadp and Zn. (pdb code 2vwq). 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 Haloferax Mediterranei Glucose Dehydrogenase in Complex with Nadp and Zn., PDB code: 2vwq:

Zinc binding site 1 out of 1 in 2vwq

Go back to Zinc Binding Sites List in 2vwq
Zinc binding site 1 out of 1 in the Haloferax Mediterranei Glucose Dehydrogenase in Complex with Nadp and Zn.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Haloferax Mediterranei Glucose Dehydrogenase in Complex with Nadp and Zn. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn800

b:44.6
occ:1.00
O A:HOH2113 1.7 34.1 1.0
NE2 A:HIS63 2.2 28.2 1.0
OE2 A:GLU64 2.3 30.6 1.0
OE1 A:GLU150 2.4 22.1 1.0
OD2 A:ASP38 2.9 43.3 1.0
CD2 A:HIS63 2.9 19.0 1.0
CD A:GLU64 3.1 22.0 1.0
CE1 A:HIS63 3.2 21.8 1.0
CD A:GLU150 3.2 20.9 1.0
CG A:GLU64 3.2 24.6 1.0
OE2 A:GLU150 3.4 21.0 1.0
CG A:ASP38 3.8 34.4 1.0
CG A:HIS63 4.1 25.7 1.0
ND1 A:HIS63 4.2 24.4 1.0
OE1 A:GLU64 4.3 28.3 1.0
OD1 A:ASP38 4.4 38.9 1.0
CG A:GLU150 4.5 19.0 1.0
CD A:PRO151 4.6 24.7 1.0
O A:HOH2112 4.6 34.6 1.0
CB A:GLU64 4.7 24.9 1.0
N A:PRO151 4.7 24.4 1.0
CB A:ASP38 4.7 39.3 1.0
CB A:PRO151 4.8 25.7 1.0
CA A:PRO151 4.8 25.1 1.0
O A:HOH2108 4.9 35.4 1.0

Reference:

P.J.Baker, K.L.Britton, M.Fisher, J.Esclapez, C.Pire, M.J.Bonete, J.Ferrer, D.W.Rice. Active Site Dynamics in the Zinc-Dependent Medium Chain Alcohol Dehydrogenase Superfamily. Proc. Natl. Acad. Sci. V. 106 779 2009U.S.A..
ISSN: ESSN 1091-6490
PubMed: 19131516
DOI: 10.1073/PNAS.0807529106
Page generated: Wed Dec 16 03:56:32 2020

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