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Atomistry » Chlorine » PDB 3v6e-3vfb » 3vbn | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 3v6e-3vfb » 3vbn » |
Chlorine in PDB 3vbn: Crystal Structure of the D94A Mutant of Antd, An N-Acyltransferase From Bacillus Cereus in Complex with Dtdp and Coenzyme AEnzymatic activity of Crystal Structure of the D94A Mutant of Antd, An N-Acyltransferase From Bacillus Cereus in Complex with Dtdp and Coenzyme A
All present enzymatic activity of Crystal Structure of the D94A Mutant of Antd, An N-Acyltransferase From Bacillus Cereus in Complex with Dtdp and Coenzyme A:
2.3.1.18; Protein crystallography data
The structure of Crystal Structure of the D94A Mutant of Antd, An N-Acyltransferase From Bacillus Cereus in Complex with Dtdp and Coenzyme A, PDB code: 3vbn
was solved by
R.L.Kubiak,
H.M.Holden,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of the D94A Mutant of Antd, An N-Acyltransferase From Bacillus Cereus in Complex with Dtdp and Coenzyme A
(pdb code 3vbn). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of the D94A Mutant of Antd, An N-Acyltransferase From Bacillus Cereus in Complex with Dtdp and Coenzyme A, PDB code: 3vbn: Chlorine binding site 1 out of 1 in 3vbnGo back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Crystal Structure of the D94A Mutant of Antd, An N-Acyltransferase From Bacillus Cereus in Complex with Dtdp and Coenzyme A
![]() Mono view ![]() Stereo pair view
Reference:
R.L.Kubiak,
H.M.Holden.
Structural Studies of Antd: An N-Acyltransferase Involved in the Biosynthesis of D-Anthrose. Biochemistry V. 51 867 2012.
Page generated: Fri Jul 11 11:38:07 2025
ISSN: ISSN 0006-2960 PubMed: 22220494 DOI: 10.1021/BI201650C |
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