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Zinc in PDB 1wxz: Crystal Structure of Adenosine Deaminase Ligated with A Potent Inhibitor

Enzymatic activity of Crystal Structure of Adenosine Deaminase Ligated with A Potent Inhibitor

All present enzymatic activity of Crystal Structure of Adenosine Deaminase Ligated with A Potent Inhibitor:
3.5.4.4;

Protein crystallography data

The structure of Crystal Structure of Adenosine Deaminase Ligated with A Potent Inhibitor, PDB code: 1wxz was solved by T.Kinoshita, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.43 / 2.80
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 77.800, 77.800, 137.400, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Other elements in 1wxz:

The structure of Crystal Structure of Adenosine Deaminase Ligated with A Potent Inhibitor also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Adenosine Deaminase Ligated with A Potent Inhibitor (pdb code 1wxz). 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 Ligated with A Potent Inhibitor, PDB code: 1wxz:

Zinc binding site 1 out of 1 in 1wxz

Go back to Zinc Binding Sites List in 1wxz
Zinc binding site 1 out of 1 in the Crystal Structure of Adenosine Deaminase Ligated with A Potent Inhibitor


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 Ligated with A Potent Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn400

b:23.4
occ:1.00
 O A:HOH423 1.9 33.1 1.0
NE2 A:HIS17 2.1 14.6 1.0
NE2 A:HIS214 2.2 15.2 1.0
NE2 A:HIS15 2.4 21.7 1.0
OD2 A:ASP295 2.8 26.7 1.0
CE1 A:HIS17 3.0 13.0 1.0
CD2 A:HIS214 3.1 14.4 1.0
CD2 A:HIS17 3.2 13.9 1.0
CE1 A:HIS15 3.2 22.2 1.0
CE1 A:HIS214 3.2 14.2 1.0
CD2 A:HIS15 3.4 22.2 1.0
OD1 A:ASP295 3.4 25.7 1.0
CG A:ASP295 3.4 25.5 1.0
O A:HOH430 3.8 8.4 1.0
NE2 A:HIS238 3.8 15.0 1.0
N30 A:FRL401 3.9 17.5 1.0
C28 A:FRL401 4.0 17.2 1.0
ND1 A:HIS17 4.1 8.5 1.0
O29 A:FRL401 4.2 19.9 1.0
CG A:HIS17 4.3 13.4 1.0
CG A:HIS214 4.3 14.8 1.0
ND1 A:HIS214 4.3 15.5 1.0
ND1 A:HIS15 4.3 22.6 1.0
O A:HOH511 4.4 3.6 1.0
CG A:HIS15 4.5 19.8 1.0
CD2 A:HIS238 4.5 14.9 1.0
C26 A:FRL401 4.7 16.6 1.0
O A:HOH528 4.8 26.2 1.0
CE1 A:HIS238 4.8 13.1 1.0
CB A:ASP295 4.9 24.0 1.0

Reference:

T.Terasaka, K.Tsuji, T.Kato, I.Nakanishi, T.Kinoshita, Y.Kato, M.Kuno, T.Inoue, K.Tanaka, K.Nakamura. Rational Design of Non-Nucleoside, Potent, and Orally Bioavailable Adenosine Deaminase Inhibitors: Predicting Enzyme Conformational Change and Metabolism J.Med.Chem. V. 48 4750 2005.
ISSN: ISSN 0022-2623
PubMed: 16033254
DOI: 10.1021/JM050413G
Page generated: Wed Oct 16 20:12:50 2024

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