Manganese in PDB 5oxj: Crystal Structure of Klentaq Mutant M747K in A Closed Ternary Complex with A O6-Meg:Benzitp Base Pair

All present enzymatic activity of Crystal Structure of Klentaq Mutant M747K in A Closed Ternary Complex with A O6-Meg:Benzitp Base Pair:
2.7.7.7;

The structure of Crystal Structure of Klentaq Mutant M747K in A Closed Ternary Complex with A O6-Meg:Benzitp Base Pair, PDB code: 5oxj was solved by K.Betz, K.Diederichs, A.Marx, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.35 / 2.00
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	109.347, 109.347, 90.636, 90.00, 90.00, 120.00
R / Rfree (%)	19.6 / 25.7

The structure of Crystal Structure of Klentaq Mutant M747K in A Closed Ternary Complex with A O6-Meg:Benzitp Base Pair also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Manganese atom in the Crystal Structure of Klentaq Mutant M747K in A Closed Ternary Complex with A O6-Meg:Benzitp Base Pair (pdb code 5oxj). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of Klentaq Mutant M747K in A Closed Ternary Complex with A O6-Meg:Benzitp Base Pair, PDB code: 5oxj:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of Klentaq Mutant M747K in A Closed Ternary Complex with A O6-Meg:Benzitp Base Pair


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Klentaq Mutant M747K in A Closed Ternary Complex with A O6-Meg:Benzitp Base Pair within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn901 b:68.6 occ:1.00 H17 A:NZI903 1.5 85.6 0.0 O A:TYR611 2.1 80.6 1.0 O11 A:NZI903 2.1 70.8 0.9 OD2 A:ASP785 2.2 66.0 1.0 O7 A:NZI903 2.4 63.2 1.0 OD1 A:ASP610 2.5 78.5 1.0 O4 A:NZI903 2.6 72.8 0.7 P1 A:NZI903 3.2 67.1 1.0 CG A:ASP785 3.3 55.4 1.0 C A:TYR611 3.3 67.3 1.0 CG A:ASP610 3.3 74.1 1.0 P2 A:NZI903 3.3 87.4 1.0 P A:NZI903 3.4 76.3 1.0 O8 A:NZI903 3.4 78.7 1.0 H6 A:NZI903 3.4 87.8 1.0 O5 A:NZI903 3.5 71.4 0.6 OD2 A:ASP610 3.5 90.8 1.0 MN A:MN902 3.6 75.1 1.0 OD1 A:ASP785 3.8 42.2 1.0 O2 A:NZI903 3.8 71.6 1.0 C4 A:NZI903 4.0 72.7 1.0 O A:HOH1016 4.1 48.5 1.0 N A:TYR611 4.1 48.0 1.0 O10 A:NZI903 4.1 91.5 1.0 CA A:SER612 4.2 65.3 1.0 N A:SER612 4.2 67.7 1.0 N A:GLN613 4.3 55.6 1.0 H7 A:NZI903 4.3 87.8 1.0 CA A:TYR611 4.3 54.3 1.0 C A:ASP610 4.4 51.3 1.0 O9 A:NZI903 4.4 85.5 1.0 C A:SER612 4.5 58.7 1.0 CB A:ASP785 4.5 36.3 1.0 CB A:ASP610 4.6 59.1 1.0 CG2 A:ILE614 4.6 48.2 1.0 O6 A:NZI903 4.7 65.0 1.0 H11 A:NZI903 4.7 0.4 1.0 O A:ASP785 4.7 50.7 1.0 O A:ASP610 4.8 48.5 1.0 O3 A:NZI903 4.8 77.8 0.8 CB A:TYR611 4.9 44.4 1.0 CA A:ASP610 4.9 47.2 1.0 N A:ILE614 5.0 43.2 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of Klentaq Mutant M747K in A Closed Ternary Complex with A O6-Meg:Benzitp Base Pair


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Klentaq Mutant M747K in A Closed Ternary Complex with A O6-Meg:Benzitp Base Pair within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn902 b:75.1 occ:1.00 O4 A:NZI903 2.0 72.8 0.7 OD2 A:ASP610 2.1 90.8 1.0 O A:HOH1004 2.2 54.3 1.0 O A:HOH1016 2.6 48.5 1.0 OD1 A:ASP785 3.1 42.2 1.0 CG A:ASP610 3.2 74.1 1.0 P A:NZI903 3.2 76.3 1.0 H17 A:NZI903 3.3 85.6 0.0 OD1 A:ASP610 3.6 78.5 1.0 OE1 A:GLU786 3.6 51.6 1.0 MN A:MN901 3.6 68.6 1.0 O3 A:NZI903 3.7 77.8 0.8 O2 A:NZI903 3.7 71.6 1.0 NZ A:LYS831 3.9 81.8 1.0 CG A:ASP785 3.9 55.4 1.0 OD2 A:ASP785 3.9 66.0 1.0 C3' B:DDG112 4.1 42.3 1.0 O11 A:NZI903 4.2 70.8 0.9 H8 A:NZI903 4.4 94.0 1.0 CB A:ASP610 4.5 59.1 1.0 CD A:GLU786 4.5 58.6 1.0 O5 A:NZI903 4.5 71.4 0.6 C5' B:DDG112 4.6 49.5 1.0 O5' B:DDG112 4.6 38.8 1.0 C4' B:DDG112 4.6 47.0 1.0 CB A:GLU786 4.7 45.6 1.0 O10 A:NZI903 4.8 91.5 1.0 OP1 B:DDG112 4.8 48.5 1.0 H11 A:NZI903 4.8 0.4 1.0 H6 A:NZI903 4.9 87.8 1.0 NZ A:LYS663 5.0 96.6 1.0 C4 A:NZI903 5.0 72.7 1.0

K.Betz, A.Nilforoushan, L.A.Wyss, K.Diederichs, S.J.Sturla, A.Marx. Structural Basis For the Selective Incorporation of An Artificial Nucleotide Opposite A Dna Adduct By A Dna Polymerase. Chem. Commun. (Camb.) V. 53 12704 2017.
ISSN: ESSN 1364-548X
PubMed: 29136072
DOI: 10.1039/C7CC07173F