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Bromine in PDB 2h34: Apoenzyme Crystal Structure of the Tuberculosis Serine/Threonine Kinase, Pkne

Enzymatic activity of Apoenzyme Crystal Structure of the Tuberculosis Serine/Threonine Kinase, Pkne

All present enzymatic activity of Apoenzyme Crystal Structure of the Tuberculosis Serine/Threonine Kinase, Pkne:
2.7.11.1;

Protein crystallography data

The structure of Apoenzyme Crystal Structure of the Tuberculosis Serine/Threonine Kinase, Pkne, PDB code: 2h34 was solved by L.M.Gay, H.L.Ng, T.Alber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.10 / 2.80
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 77.078, 77.078, 221.024, 90.00, 90.00, 120.00
R / Rfree (%) 21.6 / 26.5

Other elements in 2h34:

The structure of Apoenzyme Crystal Structure of the Tuberculosis Serine/Threonine Kinase, Pkne also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Bromine Binding Sites:

The binding sites of Bromine atom in the Apoenzyme Crystal Structure of the Tuberculosis Serine/Threonine Kinase, Pkne (pdb code 2h34). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Apoenzyme Crystal Structure of the Tuberculosis Serine/Threonine Kinase, Pkne, PDB code: 2h34:

Bromine binding site 1 out of 1 in 2h34

Go back to Bromine Binding Sites List in 2h34
Bromine binding site 1 out of 1 in the Apoenzyme Crystal Structure of the Tuberculosis Serine/Threonine Kinase, Pkne


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Apoenzyme Crystal Structure of the Tuberculosis Serine/Threonine Kinase, Pkne within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br300

b:0.0
occ:1.00
CA A:MSE104 3.9 75.5 1.0
NE2 A:GLN108 4.0 79.9 1.0
CG2 A:VAL99 4.0 67.7 1.0
CG A:MSE104 4.2 80.0 1.0
CG A:GLN108 4.3 78.3 1.0
NE A:ARG107 4.4 82.1 1.0
CB A:MSE104 4.4 75.9 1.0
CD A:GLN108 4.5 80.3 1.0
N A:MSE104 4.5 74.5 1.0
CB A:ARG107 4.6 77.3 1.0
NH2 A:ARG107 4.6 82.4 1.0
CB A:VAL99 4.8 68.4 1.0
O A:MSE104 4.8 75.4 1.0
CG1 A:VAL99 4.8 68.6 1.0
O A:ALA103 4.9 73.9 1.0
C A:MSE104 4.9 75.3 1.0
CZ A:ARG107 5.0 82.7 1.0
C A:ALA103 5.0 73.7 1.0

Reference:

L.M.Gay, H.L.Ng, T.Alber. A Conserved Dimer and Global Conformational Changes in the Structure of Apo-Pkne Ser/Thr Protein Kinase From Mycobacterium Tuberculosis. J.Mol.Biol. V. 360 409 2006.
ISSN: ISSN 0022-2836
PubMed: 16762364
DOI: 10.1016/J.JMB.2006.05.015
Page generated: Sat Dec 12 02:05:58 2020

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