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Zinc in PDB 4zga: Structural Basis For Inhibition of Human Autotaxin By Four Novel Compounds

Enzymatic activity of Structural Basis For Inhibition of Human Autotaxin By Four Novel Compounds

All present enzymatic activity of Structural Basis For Inhibition of Human Autotaxin By Four Novel Compounds:
3.1.4.39;

Protein crystallography data

The structure of Structural Basis For Inhibition of Human Autotaxin By Four Novel Compounds, PDB code: 4zga was solved by A.J.Stein, G.Bain, J.H.Hutchinson, J.F.Evans, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.74 / 2.60
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 53.672, 64.001, 70.505, 99.44, 108.39, 98.61
R / Rfree (%) 20.8 / 27.4

Other elements in 4zga:

The structure of Structural Basis For Inhibition of Human Autotaxin By Four Novel Compounds also contains other interesting chemical elements:

Fluorine (F) 1 atom
Calcium (Ca) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Structural Basis For Inhibition of Human Autotaxin By Four Novel Compounds (pdb code 4zga). 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 Structural Basis For Inhibition of Human Autotaxin By Four Novel Compounds, PDB code: 4zga:

Zinc binding site 1 out of 1 in 4zga

Go back to Zinc Binding Sites List in 4zga
Zinc binding site 1 out of 1 in the Structural Basis For Inhibition of Human Autotaxin By Four Novel Compounds


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structural Basis For Inhibition of Human Autotaxin By Four Novel Compounds within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn903

b:65.5
occ:1.00
 NE2 A:HIS475 2.1 57.5 1.0
OD1 A:ASP312 2.2 68.7 1.0
NE2 A:HIS316 2.3 66.9 1.0
C2 A:EDO905 2.4 65.7 1.0
O1 A:EDO905 2.4 72.5 1.0
C1 A:EDO905 2.6 66.7 1.0
OD2 A:ASP312 2.8 64.2 1.0
CG A:ASP312 2.8 62.0 1.0
CE1 A:HIS316 2.8 67.8 1.0
CE1 A:HIS475 2.9 57.0 1.0
CD2 A:HIS475 3.2 59.7 1.0
O2 A:EDO905 3.5 65.0 1.0
CD2 A:HIS316 3.6 67.2 1.0
CE1 A:HIS360 3.9 62.0 1.0
NE2 A:HIS360 4.1 63.1 1.0
ND1 A:HIS475 4.1 58.0 1.0
ND1 A:HIS316 4.1 73.8 1.0
CB A:ASP312 4.2 62.5 1.0
CG A:HIS475 4.3 57.2 1.0
CG A:HIS316 4.5 64.0 1.0
O A:HOH1009 4.5 48.7 1.0
OD2 A:ASP172 4.6 71.0 1.0
CE A:MET362 4.7 67.2 1.0
OG1 A:THR210 4.8 68.0 1.0
OD1 A:ASP474 4.9 75.1 1.0
OD1 A:ASP172 5.0 74.0 1.0

Reference:

A.J.Stein, G.Bain, P.Prodanovich, A.M.Santini, J.Darlington, N.M.Stelzer, R.S.Sidhu, J.Schaub, L.Goulet, D.Lonergan, I.Calderon, J.F.Evans, J.H.Hutchinson. Structural Basis For Inhibition of Human Autotaxin By Four Potent Compounds with Distinct Modes of Binding. Mol.Pharmacol. V. 88 982 2015.
ISSN: ESSN 1521-0111
PubMed: 26371182
DOI: 10.1124/MOL.115.100404
Page generated: Sun Oct 27 11:47:53 2024

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