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Atomistry » Magnesium » PDB 1l3r-1lny » 1l3v » |
Magnesium in PDB 1l3v: Crystal Structure of Bacillus Dna Polymerase I Fragment Product Complex with 15 Base Pairs of Duplex Dna Following Addition of Dttp, Datp, Dctp, and Dgtp Residues.Enzymatic activity of Crystal Structure of Bacillus Dna Polymerase I Fragment Product Complex with 15 Base Pairs of Duplex Dna Following Addition of Dttp, Datp, Dctp, and Dgtp Residues.
All present enzymatic activity of Crystal Structure of Bacillus Dna Polymerase I Fragment Product Complex with 15 Base Pairs of Duplex Dna Following Addition of Dttp, Datp, Dctp, and Dgtp Residues.:
2.7.7.7; Protein crystallography data
The structure of Crystal Structure of Bacillus Dna Polymerase I Fragment Product Complex with 15 Base Pairs of Duplex Dna Following Addition of Dttp, Datp, Dctp, and Dgtp Residues., PDB code: 1l3v
was solved by
S.J.Johnson,
J.S.Taylor,
L.S.Beese,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Bacillus Dna Polymerase I Fragment Product Complex with 15 Base Pairs of Duplex Dna Following Addition of Dttp, Datp, Dctp, and Dgtp Residues.
(pdb code 1l3v). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Bacillus Dna Polymerase I Fragment Product Complex with 15 Base Pairs of Duplex Dna Following Addition of Dttp, Datp, Dctp, and Dgtp Residues., PDB code: 1l3v: Magnesium binding site 1 out of 1 in 1l3vGo back to![]() ![]()
Magnesium binding site 1 out
of 1 in the Crystal Structure of Bacillus Dna Polymerase I Fragment Product Complex with 15 Base Pairs of Duplex Dna Following Addition of Dttp, Datp, Dctp, and Dgtp Residues.
![]() Mono view ![]() Stereo pair view
Reference:
S.J.Johnson,
J.S.Taylor,
L.S.Beese.
Processive Dna Synthesis Observed in A Polymerase Crystal Suggests A Mechanism For the Prevention of Frameshift Mutations Proc.Natl.Acad.Sci.Usa V. 100 3895 2003.
Page generated: Tue Aug 13 08:25:55 2024
ISSN: ISSN 0027-8424 PubMed: 12649320 DOI: 10.1073/PNAS.0630532100 |
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