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Zinc in PDB 2vwg: Haloferax Mediterranei Glucose Dehydrogenase in Complex with Nadp, Zn and Gluconolactone.

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

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

Protein crystallography data

The structure of Haloferax Mediterranei Glucose Dehydrogenase in Complex with Nadp, Zn and Gluconolactone., PDB code: 2vwg 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 / 2.00
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 61.647, 112.205, 150.597, 90.00, 90.00, 90.00
R / Rfree (%) 13.5 / 15.9

Zinc Binding Sites:

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

Zinc binding site 1 out of 1 in 2vwg

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


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, Zn and Gluconolactone. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn800

b:43.9
occ:0.80
 O A:HOH2143 1.8 36.2 1.0
OD2 A:ASP38 2.1 34.2 1.0
OE2 A:GLU64 2.1 36.1 1.0
NE2 A:HIS63 2.1 28.3 1.0
CG A:ASP38 2.9 36.3 1.0
CD A:GLU64 3.0 29.4 1.0
CD2 A:HIS63 3.0 26.4 1.0
CE1 A:HIS63 3.1 29.4 1.0
CG A:GLU64 3.2 24.9 1.0
OE1 A:GLU150 3.3 26.4 1.0
OD1 A:ASP38 3.6 31.7 1.0
O1 A:LGC600 3.6 33.4 1.0
O2 A:LGC600 3.7 30.9 1.0
CB A:ASP38 3.8 30.9 1.0
O A:HOH2015 3.9 37.7 1.0
OE1 A:GLU64 4.2 32.9 1.0
CG A:HIS63 4.2 28.7 1.0
ND1 A:HIS63 4.2 28.2 1.0
CD A:GLU150 4.3 28.0 1.0
C2 A:LGC600 4.4 32.6 1.0
C1 A:LGC600 4.4 33.3 1.0
OE2 A:GLU150 4.5 27.6 1.0
C5N A:NAP500 4.6 32.6 1.0
CB A:GLU64 4.7 26.4 1.0
O A:HOH2133 4.8 35.2 1.0
O A:HOH2016 4.9 28.4 1.0
NZ A:LYS349 5.0 36.5 1.0
CB A:PRO151 5.0 30.4 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: Thu Oct 17 04:38:24 2024

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