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Atomistry » Chlorine » PDB 3ser-3smc » 3slp » |
Chlorine in PDB 3slp: Crystal Structure of Lambda Exonuclease in Complex with A 12 Bp Symmetric Dna DuplexEnzymatic activity of Crystal Structure of Lambda Exonuclease in Complex with A 12 Bp Symmetric Dna Duplex
All present enzymatic activity of Crystal Structure of Lambda Exonuclease in Complex with A 12 Bp Symmetric Dna Duplex:
3.1.11.3; Protein crystallography data
The structure of Crystal Structure of Lambda Exonuclease in Complex with A 12 Bp Symmetric Dna Duplex, PDB code: 3slp
was solved by
C.E.Bell,
J.Zhang,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3slp:
The structure of Crystal Structure of Lambda Exonuclease in Complex with A 12 Bp Symmetric Dna Duplex also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Lambda Exonuclease in Complex with A 12 Bp Symmetric Dna Duplex
(pdb code 3slp). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Lambda Exonuclease in Complex with A 12 Bp Symmetric Dna Duplex, PDB code: 3slp: Jump to Chlorine binding site number: 1; 2; Chlorine binding site 1 out of 2 in 3slpGo back to![]() ![]()
Chlorine binding site 1 out
of 2 in the Crystal Structure of Lambda Exonuclease in Complex with A 12 Bp Symmetric Dna Duplex
![]() Mono view ![]() Stereo pair view
Chlorine binding site 2 out of 2 in 3slpGo back to![]() ![]()
Chlorine binding site 2 out
of 2 in the Crystal Structure of Lambda Exonuclease in Complex with A 12 Bp Symmetric Dna Duplex
![]() Mono view ![]() Stereo pair view
Reference:
J.Zhang,
K.A.Mccabe,
C.E.Bell.
Crystal Structures of {Lambda} Exonuclease in Complex with Dna Suggest An Electrostatic Ratchet Mechanism For Processivity. Proc.Natl.Acad.Sci.Usa V. 108 11872 2011.
Page generated: Fri Jul 11 10:21:46 2025
ISSN: ISSN 0027-8424 PubMed: 21730170 DOI: 10.1073/PNAS.1103467108 |
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