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Zinc in PDB 2pgf: Crystal Structure of Adenosine Deaminase From Plasmodium Vivax in Complex with Adenosine

Enzymatic activity of Crystal Structure of Adenosine Deaminase From Plasmodium Vivax in Complex with Adenosine

All present enzymatic activity of Crystal Structure of Adenosine Deaminase From Plasmodium Vivax in Complex with Adenosine:
3.5.4.4;

Protein crystallography data

The structure of Crystal Structure of Adenosine Deaminase From Plasmodium Vivax in Complex with Adenosine, PDB code: 2pgf was solved by E.T.Larson, E.A.Merritt, Structural Genomics Of Pathogenic Protozoaconsortium (Sgpp), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.00 / 1.89
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 143.962, 146.608, 50.398, 90.00, 90.00, 90.00
R / Rfree (%) 15.7 / 20.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Adenosine Deaminase From Plasmodium Vivax in Complex with Adenosine (pdb code 2pgf). 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 Crystal Structure of Adenosine Deaminase From Plasmodium Vivax in Complex with Adenosine, PDB code: 2pgf:

Zinc binding site 1 out of 1 in 2pgf

Go back to Zinc Binding Sites List in 2pgf
Zinc binding site 1 out of 1 in the Crystal Structure of Adenosine Deaminase From Plasmodium Vivax in Complex with Adenosine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Adenosine Deaminase From Plasmodium Vivax in Complex with Adenosine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:46.8
occ:0.60
 NE2 A:HIS42 2.1 22.1 1.0
NE2 A:HIS44 2.2 23.2 1.0
NE2 A:HIS226 2.3 22.5 1.0
OD1 A:ASP310 2.4 18.9 1.0
CD2 A:HIS44 3.0 21.6 1.0
CE1 A:HIS42 3.1 24.1 1.0
CD2 A:HIS42 3.1 22.1 1.0
N6 A:ADN501 3.2 35.2 1.0
CD2 A:HIS226 3.2 25.3 1.0
C6 A:ADN501 3.2 34.6 1.0
CE1 A:HIS44 3.2 21.2 1.0
CE1 A:HIS226 3.2 26.0 1.0
C5 A:ADN501 3.3 32.7 1.0
CG A:ASP310 3.4 23.9 1.0
N7 A:ADN501 3.4 30.4 1.0
NE2 A:HIS253 3.7 28.0 1.0
OD2 A:ASP310 3.8 24.7 1.0
N1 A:ADN501 4.0 31.8 1.0
C4 A:ADN501 4.1 29.9 1.0
ND1 A:HIS42 4.2 23.9 1.0
CG A:HIS42 4.2 22.5 1.0
CG A:HIS44 4.2 18.8 1.0
C8 A:ADN501 4.2 28.9 1.0
ND1 A:HIS44 4.3 20.7 1.0
ND1 A:HIS226 4.3 25.2 1.0
CG A:HIS226 4.3 24.8 1.0
CD2 A:HIS253 4.3 27.6 1.0
N9 A:ADN501 4.6 31.3 1.0
C2 A:ADN501 4.6 29.7 1.0
CE1 A:HIS253 4.7 25.8 1.0
OD2 A:ASP311 4.7 23.3 1.0
N3 A:ADN501 4.7 29.9 1.0
CB A:ASP310 4.7 19.0 1.0
CA A:ASP310 4.9 18.3 1.0

Reference:

E.T.Larson, W.Deng, B.E.Krumm, A.Napuli, N.Mueller, W.C.Van Voorhis, F.S.Buckner, E.Fan, A.Lauricella, G.Detitta, J.Luft, F.Zucker, W.G.Hol, C.L.Verlinde, E.A.Merritt. Structures of Substrate- and Inhibitor-Bound Adenosine Deaminase From A Human Malaria Parasite Show A Dramatic Conformational Change and Shed Light on Drug Selectivity. J.Mol.Biol. V. 381 975 2008.
ISSN: ISSN 0022-2836
PubMed: 18602399
DOI: 10.1016/J.JMB.2008.06.048
Page generated: Wed Dec 16 03:48:03 2020

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