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Manganese in PDB 3px6: Crystal Structure of Bacillus Dna Polymerase I Large Fragment Bound to Dna and Ddctp-Da Mismatch (Tautomer) in Closed Conformation

Enzymatic activity of Crystal Structure of Bacillus Dna Polymerase I Large Fragment Bound to Dna and Ddctp-Da Mismatch (Tautomer) in Closed Conformation

All present enzymatic activity of Crystal Structure of Bacillus Dna Polymerase I Large Fragment Bound to Dna and Ddctp-Da Mismatch (Tautomer) in Closed Conformation:
2.7.7.7;

Protein crystallography data

The structure of Crystal Structure of Bacillus Dna Polymerase I Large Fragment Bound to Dna and Ddctp-Da Mismatch (Tautomer) in Closed Conformation, PDB code: 3px6 was solved by W.Wang, L.S.Beese, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 87.75 / 1.59
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 93.460, 108.280, 149.760, 90.00, 90.00, 90.00
R / Rfree (%) 18.5 / 20.7

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Bacillus Dna Polymerase I Large Fragment Bound to Dna and Ddctp-Da Mismatch (Tautomer) in Closed Conformation (pdb code 3px6). 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 Bacillus Dna Polymerase I Large Fragment Bound to Dna and Ddctp-Da Mismatch (Tautomer) in Closed Conformation, PDB code: 3px6:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 3px6

Go back to Manganese Binding Sites List in 3px6
Manganese binding site 1 out of 2 in the Crystal Structure of Bacillus Dna Polymerase I Large Fragment Bound to Dna and Ddctp-Da Mismatch (Tautomer) in Closed Conformation


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 Bacillus Dna Polymerase I Large Fragment Bound to Dna and Ddctp-Da Mismatch (Tautomer) in Closed Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1

b:22.1
occ:1.00
OD2 A:ASP830 2.1 23.3 1.0
O2B A:DCT201 2.1 23.4 1.0
O2G A:DCT201 2.2 22.8 1.0
O1A A:DCT201 2.2 18.6 1.0
OD1 A:ASP653 2.2 27.9 1.0
O A:TYR654 2.2 25.1 1.0
CG A:ASP830 3.2 27.7 1.0
PB A:DCT201 3.2 21.5 1.0
CG A:ASP653 3.3 33.6 1.0
C A:TYR654 3.4 29.3 1.0
PG A:DCT201 3.4 23.3 1.0
PA A:DCT201 3.4 21.2 1.0
O3B A:DCT201 3.6 22.7 1.0
OD1 A:ASP830 3.6 22.1 1.0
OD2 A:ASP653 3.6 33.9 1.0
O3A A:DCT201 3.7 21.6 1.0
O A:HOH967 3.8 23.1 1.0
HG22 A:ILE657 3.8 30.4 1.0
H A:ILE657 3.9 30.9 1.0
HA A:SER655 4.0 34.7 1.0
O A:HOH1050 4.0 36.1 1.0
HB2 A:TYR654 4.1 24.7 1.0
H A:GLN656 4.1 30.9 1.0
N A:TYR654 4.1 24.1 1.0
CA A:TYR654 4.2 23.4 1.0
H A:TYR654 4.2 28.8 1.0
HB A:ILE657 4.2 31.8 1.0
C5' A:DCT201 4.2 20.2 1.0
O3G A:DCT201 4.3 29.4 1.0
N A:SER655 4.3 28.1 1.0
O A:HOH254 4.3 33.6 1.0
O5' A:DCT201 4.4 20.1 1.0
O1G A:DCT201 4.4 25.8 1.0
N A:GLN656 4.5 25.8 1.0
CB A:ASP830 4.5 23.4 1.0
HB2 A:ASP830 4.5 28.1 1.0
HG21 A:ILE657 4.5 30.4 1.0
CA A:SER655 4.5 29.0 1.0
C A:ASP653 4.5 29.1 1.0
CG2 A:ILE657 4.5 25.4 1.0
CB A:ASP653 4.6 25.3 1.0
O1B A:DCT201 4.6 23.4 1.0
CB A:TYR654 4.6 20.6 1.0
O2A A:DCT201 4.6 25.0 1.0
C A:SER655 4.7 26.5 1.0
N A:ILE657 4.7 25.7 1.0
HB3 A:TYR654 4.7 24.7 1.0
HB3 A:ASP653 4.8 30.3 1.0
O A:ASP830 4.8 24.6 1.0
CB A:ILE657 4.9 26.6 1.0
HB3 A:ASP830 4.9 28.1 1.0
HA A:ASP653 4.9 28.2 1.0
CA A:ASP653 5.0 23.5 1.0

Manganese binding site 2 out of 2 in 3px6

Go back to Manganese Binding Sites List in 3px6
Manganese binding site 2 out of 2 in the Crystal Structure of Bacillus Dna Polymerase I Large Fragment Bound to Dna and Ddctp-Da Mismatch (Tautomer) in Closed Conformation


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 Bacillus Dna Polymerase I Large Fragment Bound to Dna and Ddctp-Da Mismatch (Tautomer) in Closed Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn2

b:14.8
occ:1.00
OD2 D:ASP830 2.1 16.2 1.0
O D:TYR654 2.2 17.2 1.0
O2G D:DCT202 2.2 17.4 1.0
OD1 D:ASP653 2.2 20.7 1.0
O1A D:DCT202 2.3 16.0 1.0
O2B D:DCT202 2.3 15.3 1.0
CG D:ASP830 3.1 15.8 1.0
PB D:DCT202 3.3 16.0 1.0
CG D:ASP653 3.3 28.7 1.0
C D:TYR654 3.4 14.1 1.0
PG D:DCT202 3.4 17.8 1.0
PA D:DCT202 3.5 15.9 1.0
O3B D:DCT202 3.6 17.9 1.0
OD1 D:ASP830 3.6 14.7 1.0
O D:HOH116 3.6 22.0 1.0
HA D:SER655 3.7 16.3 0.5
OD2 D:ASP653 3.7 31.2 1.0
O3A D:DCT202 3.8 16.5 1.0
HA D:SER655 3.9 16.4 0.5
H D:GLN656 3.9 18.4 0.5
H D:GLN656 3.9 18.4 0.5
H D:ILE657 3.9 19.1 1.0
HG22 D:ILE657 4.0 22.7 1.0
HB D:ILE657 4.1 21.8 1.0
HB2 D:TYR654 4.2 15.6 1.0
O D:HOH246 4.2 35.3 1.0
N D:TYR654 4.2 10.5 1.0
N D:SER655 4.3 12.1 0.5
C5' D:DCT202 4.3 16.3 1.0
N D:SER655 4.3 12.1 0.5
HB2 D:ASP830 4.3 17.5 1.0
CA D:SER655 4.3 13.6 0.5
H D:TYR654 4.3 12.5 1.0
CA D:TYR654 4.3 11.7 1.0
CB D:ASP830 4.3 14.6 1.0
O3G D:DCT202 4.3 21.0 1.0
N D:GLN656 4.3 15.4 1.0
O D:HOH215 4.4 28.4 1.0
CA D:SER655 4.4 13.7 0.5
O1G D:DCT202 4.4 17.0 1.0
O5' D:DCT202 4.4 14.5 1.0
HG21 D:ILE657 4.5 22.7 1.0
C D:SER655 4.6 15.1 0.5
CG2 D:ILE657 4.6 19.0 1.0
C D:SER655 4.6 15.0 0.5
C D:ASP653 4.6 18.0 1.0
O2A D:DCT202 4.6 18.7 1.0
O1B D:DCT202 4.7 13.4 1.0
CB D:ASP653 4.7 16.4 1.0
CB D:TYR654 4.7 13.0 1.0
N D:ILE657 4.7 15.9 1.0
HB3 D:ASP830 4.8 17.5 1.0
CB D:ILE657 4.8 18.2 1.0
O D:ASP830 4.8 13.6 1.0
HB3 D:TYR654 4.9 15.6 1.0
O D:HOH160 4.9 26.6 1.0
HZ3 D:LYS706 4.9 28.2 1.0
HB3 D:ASP653 5.0 19.7 1.0

Reference:

W.Wang, H.W.Hellinga, L.S.Beese. Structural Evidence For the Rare Tautomer Hypothesis of Spontaneous Mutagenesis. Proc.Natl.Acad.Sci.Usa V. 108 17644 2011.
ISSN: ISSN 0027-8424
PubMed: 22006298
DOI: 10.1073/PNAS.1114496108
Page generated: Sat Oct 5 17:33:43 2024

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