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Chlorine in PDB 3b0x: K263A Mutant of Polx From Thermus Thermophilus HB8 Complexed with Ca- Dgtp

Enzymatic activity of K263A Mutant of Polx From Thermus Thermophilus HB8 Complexed with Ca- Dgtp

All present enzymatic activity of K263A Mutant of Polx From Thermus Thermophilus HB8 Complexed with Ca- Dgtp:
2.7.7.7;

Protein crystallography data

The structure of K263A Mutant of Polx From Thermus Thermophilus HB8 Complexed with Ca- Dgtp, PDB code: 3b0x was solved by S.Nakane, N.Nakagawa, R.Masui, S.Kuramitsu, Riken Structuralgenomics/Proteomics Initiative (Rsgi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.36
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 69.088, 53.202, 84.859, 90.00, 107.65, 90.00
R / Rfree (%) 17.1 / 19.8

Other elements in 3b0x:

The structure of K263A Mutant of Polx From Thermus Thermophilus HB8 Complexed with Ca- Dgtp also contains other interesting chemical elements:

Calcium (Ca) 4 atoms
Zinc (Zn) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the K263A Mutant of Polx From Thermus Thermophilus HB8 Complexed with Ca- Dgtp (pdb code 3b0x). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the K263A Mutant of Polx From Thermus Thermophilus HB8 Complexed with Ca- Dgtp, PDB code: 3b0x:

Chlorine binding site 1 out of 1 in 3b0x

Go back to Chlorine Binding Sites List in 3b0x
Chlorine binding site 1 out of 1 in the K263A Mutant of Polx From Thermus Thermophilus HB8 Complexed with Ca- Dgtp


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of K263A Mutant of Polx From Thermus Thermophilus HB8 Complexed with Ca- Dgtp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl582

b:21.7
occ:1.00
N A:GLU297 3.3 11.7 1.0
O A:HOH634 3.3 17.0 1.0
NH1 A:ARG182 3.5 21.3 1.0
O A:HOH1108 3.6 35.0 1.0
CA A:THR296 3.6 12.4 1.0
CB A:THR296 3.6 13.3 1.0
CD1 A:LEU256 3.8 13.7 1.0
C A:THR296 4.0 11.2 1.0
CG2 A:THR296 4.2 16.7 1.0
CB A:GLU297 4.2 13.2 1.0
NH2 A:ARG182 4.2 23.0 1.0
CZ A:ARG182 4.3 19.1 1.0
CA A:GLU297 4.4 11.5 1.0
CD2 A:TYR252 4.6 10.8 1.0
O A:GLU295 4.6 13.6 1.0
CE2 A:TYR252 4.7 11.8 1.0
CA A:GLY253 4.8 10.0 1.0
OG1 A:THR296 4.8 14.8 1.0
N A:THR296 4.9 12.8 1.0

Reference:

S.Nakane, H.Ishikawa, N.Nakagawa, S.Kuramitsu, R.Masui. The Structural Basis of the Kinetic Mechanism of A Gap-Filling X-Family Dna Polymerase That Binds Mg(2+)-Dntp Before Binding to Dna. J.Mol.Biol. V. 417 179 2012.
ISSN: ISSN 0022-2836
PubMed: 22306405
DOI: 10.1016/J.JMB.2012.01.025
Page generated: Sat Dec 12 09:32:44 2020

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