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Atomistry » Magnesium » PDB 1l3r-1lny » 1l3t » |
Magnesium in PDB 1l3t: Crystal Structure of Bacillus Dna Polymerase I Fragment Product Complex with 10 Base Pairs of Duplex Dna Following Addition of A Single Dttp ResidueEnzymatic activity of Crystal Structure of Bacillus Dna Polymerase I Fragment Product Complex with 10 Base Pairs of Duplex Dna Following Addition of A Single Dttp Residue
All present enzymatic activity of Crystal Structure of Bacillus Dna Polymerase I Fragment Product Complex with 10 Base Pairs of Duplex Dna Following Addition of A Single Dttp Residue:
2.7.7.7; Protein crystallography data
The structure of Crystal Structure of Bacillus Dna Polymerase I Fragment Product Complex with 10 Base Pairs of Duplex Dna Following Addition of A Single Dttp Residue, PDB code: 1l3t
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 10 Base Pairs of Duplex Dna Following Addition of A Single Dttp Residue
(pdb code 1l3t). 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 10 Base Pairs of Duplex Dna Following Addition of A Single Dttp Residue, PDB code: 1l3t: Magnesium binding site 1 out of 1 in 1l3tGo back to![]() ![]()
Magnesium binding site 1 out
of 1 in the Crystal Structure of Bacillus Dna Polymerase I Fragment Product Complex with 10 Base Pairs of Duplex Dna Following Addition of A Single Dttp Residue
![]() 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: Sun Aug 10 00:37:34 2025
ISSN: ISSN 0027-8424 PubMed: 12649320 DOI: 10.1073/PNAS.0630532100 |
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