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Fluorine in PDB 1z35: Crystal Structure of Trichomonas Vaginalis Purine Nucleoside Phosphorylase Complexed with 2-Fluoroadenosine

Enzymatic activity of Crystal Structure of Trichomonas Vaginalis Purine Nucleoside Phosphorylase Complexed with 2-Fluoroadenosine

All present enzymatic activity of Crystal Structure of Trichomonas Vaginalis Purine Nucleoside Phosphorylase Complexed with 2-Fluoroadenosine:
2.4.2.1;

Protein crystallography data

The structure of Crystal Structure of Trichomonas Vaginalis Purine Nucleoside Phosphorylase Complexed with 2-Fluoroadenosine, PDB code: 1z35 was solved by Y.Zhang, W.H.Wang, S.W.Wu, C.C.Wang, S.E.Ealick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.56 / 2.50
Space group P 41 3 2
Cell size a, b, c (Å), α, β, γ (°) 136.800, 136.800, 136.800, 90.00, 90.00, 90.00
R / Rfree (%) 20.4 / 24.4

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of Trichomonas Vaginalis Purine Nucleoside Phosphorylase Complexed with 2-Fluoroadenosine (pdb code 1z35). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Crystal Structure of Trichomonas Vaginalis Purine Nucleoside Phosphorylase Complexed with 2-Fluoroadenosine, PDB code: 1z35:

Fluorine binding site 1 out of 1 in 1z35

Go back to Fluorine Binding Sites List in 1z35
Fluorine binding site 1 out of 1 in the Crystal Structure of Trichomonas Vaginalis Purine Nucleoside Phosphorylase Complexed with 2-Fluoroadenosine


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Trichomonas Vaginalis Purine Nucleoside Phosphorylase Complexed with 2-Fluoroadenosine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F300

b:41.0
occ:1.00
F A:2FA300 0.0 41.0 1.0
C2 A:2FA300 1.3 40.0 1.0
N1 A:2FA300 2.3 39.0 1.0
N3 A:2FA300 2.3 39.9 1.0
CG2 A:THR156 3.4 29.9 1.0
CG1 A:VAL178 3.4 36.1 1.0
C4 A:2FA300 3.5 38.1 1.0
C6 A:2FA300 3.5 38.6 1.0
CG A:MET180 3.7 28.1 1.0
CD1 A:PHE159 3.7 31.3 1.0
O A:HOH306 3.7 42.2 1.0
O A:GLU179 3.9 25.5 1.0
SD A:MET180 4.0 31.2 1.0
C5 A:2FA300 4.1 37.7 1.0
C A:GLU179 4.2 30.3 1.0
CE1 A:PHE159 4.3 30.3 1.0
CA A:PHE159 4.3 31.5 1.0
CA A:GLU179 4.3 31.6 1.0
CB A:VAL178 4.3 37.1 1.0
O A:VAL178 4.4 33.9 1.0
C A:VAL178 4.4 34.0 1.0
N A:GLU179 4.4 31.3 1.0
CG A:PHE159 4.5 31.7 1.0
N6 A:2FA300 4.6 38.7 1.0
CB A:PHE159 4.6 32.6 1.0
CB A:THR156 4.8 31.3 1.0
N9 A:2FA300 4.8 39.1 1.0
C5' A:2FA300 4.9 36.5 1.0

Reference:

Y.Zang, W.H.Wang, S.W.Wu, S.E.Ealick, C.C.Wang. Identification of A Subversive Substrate of Trichomonas Vaginalis Purine Nucleoside Phosphorylase and the Crystal Structure of the Enzyme-Substrate Complex. J.Biol.Chem. V. 280 22318 2005.
ISSN: ISSN 0021-9258
PubMed: 15817485
DOI: 10.1074/JBC.M501843200
Page generated: Sun Dec 13 11:34:24 2020

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