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Zinc in PDB 4y12: Crystal Structure of the S/T Protein Kinase Pkng From Mycobacterium Tuberculosis in Complex with Ags

Enzymatic activity of Crystal Structure of the S/T Protein Kinase Pkng From Mycobacterium Tuberculosis in Complex with Ags

All present enzymatic activity of Crystal Structure of the S/T Protein Kinase Pkng From Mycobacterium Tuberculosis in Complex with Ags:
2.7.11.1;

Protein crystallography data

The structure of Crystal Structure of the S/T Protein Kinase Pkng From Mycobacterium Tuberculosis in Complex with Ags, PDB code: 4y12 was solved by M.N.Lisa, P.M.Alzari, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.90 / 1.90
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 75.452, 37.183, 108.032, 90.00, 97.93, 90.00
R / Rfree (%) 19.6 / 21.2

Other elements in 4y12:

The structure of Crystal Structure of the S/T Protein Kinase Pkng From Mycobacterium Tuberculosis in Complex with Ags also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the S/T Protein Kinase Pkng From Mycobacterium Tuberculosis in Complex with Ags (pdb code 4y12). 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 the S/T Protein Kinase Pkng From Mycobacterium Tuberculosis in Complex with Ags, PDB code: 4y12:

Zinc binding site 1 out of 1 in 4y12

Go back to Zinc Binding Sites List in 4y12
Zinc binding site 1 out of 1 in the Crystal Structure of the S/T Protein Kinase Pkng From Mycobacterium Tuberculosis in Complex with Ags


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 the S/T Protein Kinase Pkng From Mycobacterium Tuberculosis in Complex with Ags within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn502

b:48.7
occ:1.00
 SG A:CYS128 2.2 39.8 1.0
SG A:CYS131 2.3 40.9 1.0
SG A:CYS109 2.4 44.5 1.0
SG A:CYS106 2.4 36.6 1.0
CB A:CYS128 3.0 34.4 1.0
CB A:CYS106 3.2 32.6 1.0
CB A:CYS109 3.3 44.6 1.0
CB A:CYS131 3.4 41.3 1.0
N A:CYS131 3.8 42.2 1.0
N A:CYS109 3.8 43.7 1.0
CA A:CYS109 4.1 44.9 1.0
CA A:CYS131 4.1 42.1 1.0
CA A:CYS128 4.4 32.8 1.0
CA A:CYS106 4.7 32.9 1.0
CB A:ASN108 4.7 46.1 1.0
C A:CYS131 4.8 42.4 1.0
C A:TYR130 4.8 48.5 1.0
N A:GLY132 4.8 37.4 1.0
C A:ASN108 4.8 49.6 1.0
CB A:SER133 4.8 36.2 1.0
C A:CYS109 4.8 46.4 1.0
CB A:TYR130 4.9 44.3 1.0
N A:SER133 4.9 35.2 1.0
ND2 A:ASN108 4.9 51.4 1.0
C A:CYS128 4.9 42.1 1.0

Reference:

M.N.Lisa, M.Gil, G.Andre-Leroux, N.Barilone, R.Duran, R.M.Biondi, P.M.Alzari. Molecular Basis of the Activity and the Regulation of the Eukaryotic-Like S/T Protein Kinase Pkng From Mycobacterium Tuberculosis. Structure 2015.
ISSN: ISSN 0969-2126
PubMed: 25960409
DOI: 10.1016/J.STR.2015.04.001
Page generated: Wed Dec 16 05:55:57 2020

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