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Zinc in PDB 2ai3: Purine Nucleoside Phosphorylase From Calf Spleen

Enzymatic activity of Purine Nucleoside Phosphorylase From Calf Spleen

All present enzymatic activity of Purine Nucleoside Phosphorylase From Calf Spleen:
2.4.2.1;

Protein crystallography data

The structure of Purine Nucleoside Phosphorylase From Calf Spleen, PDB code: 2ai3 was solved by A.V.Toms, W.Wang, Y.Li, B.Ganem, S.E.Ealick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 31.33 / 1.70
Space group P 21 3
Cell size a, b, c (Å), α, β, γ (°) 93.992, 93.992, 93.992, 90.00, 90.00, 90.00
R / Rfree (%) 22.1 / 25.3

Other elements in 2ai3:

The structure of Purine Nucleoside Phosphorylase From Calf Spleen also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Purine Nucleoside Phosphorylase From Calf Spleen (pdb code 2ai3). 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 Purine Nucleoside Phosphorylase From Calf Spleen, PDB code: 2ai3:

Zinc binding site 1 out of 1 in 2ai3

Go back to Zinc Binding Sites List in 2ai3
Zinc binding site 1 out of 1 in the Purine Nucleoside Phosphorylase From Calf Spleen


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Purine Nucleoside Phosphorylase From Calf Spleen within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn291

b:5.1
occ:0.33
NE2 A:HIS20 2.2 19.5 1.0
O A:HOH2096 2.8 25.6 0.3
CD2 A:HIS20 3.0 19.9 1.0
CE1 A:HIS20 3.3 19.2 1.0
CG A:HIS20 4.2 15.9 1.0
ND1 A:HIS20 4.3 18.2 1.0
O A:HOH2003 4.3 24.8 1.0
NE1 A:TRP16 4.6 19.7 1.0
O A:HOH2097 4.8 28.4 1.0
CZ2 A:TRP16 4.8 16.8 1.0
CE2 A:TRP16 5.0 21.9 1.0

Reference:

A.V.Toms, W.Wang, Y.Li, B.Ganem, S.E.Ealick. Novel Multisubstrate Inhibitors of Mammalian Purine Nucleoside Phosphorylase. Acta Crystallogr.,Sect.D V. 61 1449 2005.
ISSN: ISSN 0907-4449
PubMed: 16239721
DOI: 10.1107/S0907444905025503
Page generated: Wed Dec 16 03:17:37 2020

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