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Platinum in PDB 6mxo: Structure of Hpoleta Incorporating Dctp Opposite the 3-Prime Pt(Dach)- Gg

Enzymatic activity of Structure of Hpoleta Incorporating Dctp Opposite the 3-Prime Pt(Dach)- Gg

All present enzymatic activity of Structure of Hpoleta Incorporating Dctp Opposite the 3-Prime Pt(Dach)- Gg:
2.7.7.7;

Protein crystallography data

The structure of Structure of Hpoleta Incorporating Dctp Opposite the 3-Prime Pt(Dach)- Gg, PDB code: 6mxo was solved by H.Ouzon-Shubeita, S.Lee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.86 / 2.04
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 98.560, 98.560, 81.713, 90.00, 90.00, 120.00
R / Rfree (%) 17.5 / 23

Other elements in 6mxo:

The structure of Structure of Hpoleta Incorporating Dctp Opposite the 3-Prime Pt(Dach)- Gg also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Platinum Binding Sites:

The binding sites of Platinum atom in the Structure of Hpoleta Incorporating Dctp Opposite the 3-Prime Pt(Dach)- Gg (pdb code 6mxo). This binding sites where shown within 5.0 Angstroms radius around Platinum atom.
In total only one binding site of Platinum was determined in the Structure of Hpoleta Incorporating Dctp Opposite the 3-Prime Pt(Dach)- Gg, PDB code: 6mxo:

Platinum binding site 1 out of 1 in 6mxo

Go back to Platinum Binding Sites List in 6mxo
Platinum binding site 1 out of 1 in the Structure of Hpoleta Incorporating Dctp Opposite the 3-Prime Pt(Dach)- Gg


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 1 of Structure of Hpoleta Incorporating Dctp Opposite the 3-Prime Pt(Dach)- Gg within 5.0Å range:
probe atom residue distance (Å) B Occ
T:Pt101

b:26.3
occ:1.00
 PT T:9RD101 0.0 26.3 1.0
N1 T:9RD101 1.8 35.6 1.0
N7 T:DG4 1.9 22.5 0.4
N7 T:DG3 1.9 30.7 0.6
N7 T:DG4 1.9 22.4 0.6
N2 T:9RD101 2.0 35.9 1.0
N7 T:DG3 2.0 19.7 0.4
C8 T:DG3 2.8 33.0 0.6
C8 T:DG4 2.9 20.8 0.4
C8 T:DG4 2.9 20.4 0.6
C2 T:9RD101 2.9 38.6 1.0
C1 T:9RD101 2.9 38.0 1.0
C5 T:DG3 2.9 33.3 0.6
C5 T:DG4 3.0 21.0 0.4
C8 T:DG3 3.0 19.4 0.4
C5 T:DG4 3.0 21.0 0.6
C5 T:DG3 3.1 18.1 0.4
O6 T:DG4 3.3 21.0 0.4
O6 T:DG3 3.4 17.8 0.4
O6 T:DG4 3.4 21.0 0.6
O6 T:DG3 3.4 35.0 0.6
C6 T:DG4 3.5 21.4 0.4
C6 T:DG3 3.5 32.6 0.6
C6 T:DG4 3.5 21.7 0.6
C6 T:DG3 3.6 17.9 0.4
N9 T:DG3 4.0 34.4 0.6
C4 T:DG3 4.0 33.1 0.6
N9 T:DG4 4.1 20.3 0.4
N9 T:DG4 4.1 20.1 0.6
C4 T:DG4 4.1 20.1 0.4
O T:HOH207 4.1 27.1 1.0
C4 T:DG4 4.1 19.6 0.6
N9 T:DG3 4.2 20.0 0.4
O T:HOH211 4.2 22.3 1.0
C4 T:DG3 4.2 18.8 0.4
C6 T:9RD101 4.2 40.8 1.0
C3 T:9RD101 4.3 42.5 1.0
OP1 T:DG3 4.3 48.4 0.6
N4 T:DC5 4.5 20.9 1.0
NH1 A:ARG61 4.8 28.0 0.5
N1 T:DG3 4.8 33.6 0.6
N1 T:DG4 4.9 19.8 0.4
N1 T:DG4 4.9 19.2 0.6
N1 T:DG3 4.9 17.4 0.4

Reference:

H.Ouzon-Shubeita, M.Baker, M.C.Koag, S.Lee. Structural Basis For the Bypass of the Major Oxaliplatin-Dna Adducts By Human Dna Polymerase Eta. Biochem. J. V. 476 747 2019.
ISSN: ESSN 1470-8728
PubMed: 30709915
DOI: 10.1042/BCJ20180848
Page generated: Wed Dec 16 02:05:39 2020

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