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Manganese in PDB 6vdc: Pol Domain of POL1 From M. Smegmatis

Enzymatic activity of Pol Domain of POL1 From M. Smegmatis

All present enzymatic activity of Pol Domain of POL1 From M. Smegmatis:
2.7.7.7;

Protein crystallography data

The structure of Pol Domain of POL1 From M. Smegmatis, PDB code: 6vdc was solved by S.Shuman, Y.Goldgur, S.Ghosh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.83 / 2.40
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 62.591, 150.951, 150.348, 90.00, 90.00, 90.00
R / Rfree (%) 21.9 / 26.6

Manganese Binding Sites:

The binding sites of Manganese atom in the Pol Domain of POL1 From M. Smegmatis (pdb code 6vdc). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Pol Domain of POL1 From M. Smegmatis, PDB code: 6vdc:

Manganese binding site 1 out of 1 in 6vdc

Go back to Manganese Binding Sites List in 6vdc
Manganese binding site 1 out of 1 in the Pol Domain of POL1 From M. Smegmatis


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Pol Domain of POL1 From M. Smegmatis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1001

b:75.9
occ:1.00
OD2 A:ASP367 1.6 74.2 1.0
O A:HOH1102 2.2 67.3 1.0
NE2 A:HIS337 2.3 66.6 1.0
OD2 A:ASP369 2.4 66.5 1.0
O A:HOH1152 2.5 79.0 1.0
CG A:ASP367 2.8 74.1 1.0
O A:HOH1177 2.8 73.1 1.0
CD2 A:HIS337 3.1 64.8 1.0
CG A:ASP369 3.2 67.8 1.0
CE1 A:HIS337 3.3 68.3 1.0
OD1 A:ASP367 3.5 83.4 1.0
OE1 A:GLU336 3.6 76.5 1.0
CB A:ASP367 3.8 67.2 1.0
CB A:ASP369 3.9 63.7 1.0
OD1 A:ASP369 3.9 66.5 1.0
CG A:HIS337 4.3 70.9 1.0
ND1 A:HIS337 4.3 69.1 1.0
CD A:GLU336 4.5 79.6 1.0

Reference:

S.Ghosh, Y.Goldgur, S.Shuman. Mycobacterial Dna Polymerase I: Activities and Crystal Structures of the Pol Domain As Apoenzyme and in Complex with A Dna Primer-Template and of the Full-Length Fen/Exo-Pol Enzyme Nucleic Acids Res. 2020.
ISSN: ESSN 1362-4962
Page generated: Tue Dec 15 05:04:34 2020

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