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Atomistry » Magnesium » PDB 1l3r-1lny » 1l5u » |
Magnesium in PDB 1l5u: Crystal Structure of Bacillus Dna Polymerase I Fragment Product Complex with 12 Base Pairs of Duplex Dna Following Addition of A Dttp, A Datp, and A Dctp Residue.Enzymatic activity of Crystal Structure of Bacillus Dna Polymerase I Fragment Product Complex with 12 Base Pairs of Duplex Dna Following Addition of A Dttp, A Datp, and A Dctp Residue.
All present enzymatic activity of Crystal Structure of Bacillus Dna Polymerase I Fragment Product Complex with 12 Base Pairs of Duplex Dna Following Addition of A Dttp, A Datp, and A Dctp Residue.:
2.7.7.7; Protein crystallography data
The structure of Crystal Structure of Bacillus Dna Polymerase I Fragment Product Complex with 12 Base Pairs of Duplex Dna Following Addition of A Dttp, A Datp, and A Dctp Residue., PDB code: 1l5u
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 12 Base Pairs of Duplex Dna Following Addition of A Dttp, A Datp, and A Dctp Residue.
(pdb code 1l5u). 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 12 Base Pairs of Duplex Dna Following Addition of A Dttp, A Datp, and A Dctp Residue., PDB code: 1l5u: Magnesium binding site 1 out of 1 in 1l5uGo back to Magnesium Binding Sites List in 1l5u
Magnesium binding site 1 out
of 1 in the Crystal Structure of Bacillus Dna Polymerase I Fragment Product Complex with 12 Base Pairs of Duplex Dna Following Addition of A Dttp, A Datp, and A Dctp 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: Tue Aug 13 08:26:25 2024
ISSN: ISSN 0027-8424 PubMed: 12649320 DOI: 10.1073/PNAS.0630532100 |
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