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Chlorine in PDB 5upq: Acyl-Coa Synthetase PTMA2 From Streptomyces Platensis in Complex with SBNP465 LigandProtein crystallography data
The structure of Acyl-Coa Synthetase PTMA2 From Streptomyces Platensis in Complex with SBNP465 Ligand, PDB code: 5upq
was solved by
J.Osipiuk,
C.Hatzos-Skintges,
M.Endres,
G.Babnigg,
J.D.Rudolf,
C.Y.Chang,
M.Ma,
B.Shen,
G.N.Phillips Jr.,
A.Joachimiak,
Midwest Center Forstructural Genomics (Mcsg),
Enzyme Discovery For Natural Productbiosynthesis (Natpro),
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 Acyl-Coa Synthetase PTMA2 From Streptomyces Platensis in Complex with SBNP465 Ligand
(pdb code 5upq). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Acyl-Coa Synthetase PTMA2 From Streptomyces Platensis in Complex with SBNP465 Ligand, PDB code: 5upq: Jump to Chlorine binding site number: 1; 2; 3; Chlorine binding site 1 out of 3 in 5upqGo back to Chlorine Binding Sites List in 5upq
Chlorine binding site 1 out
of 3 in the Acyl-Coa Synthetase PTMA2 From Streptomyces Platensis in Complex with SBNP465 Ligand
Mono view Stereo pair view
Chlorine binding site 2 out of 3 in 5upqGo back to Chlorine Binding Sites List in 5upq
Chlorine binding site 2 out
of 3 in the Acyl-Coa Synthetase PTMA2 From Streptomyces Platensis in Complex with SBNP465 Ligand
Mono view Stereo pair view
Chlorine binding site 3 out of 3 in 5upqGo back to Chlorine Binding Sites List in 5upq
Chlorine binding site 3 out
of 3 in the Acyl-Coa Synthetase PTMA2 From Streptomyces Platensis in Complex with SBNP465 Ligand
Mono view Stereo pair view
Reference:
N.Wang,
J.D.Rudolf,
L.B.Dong,
J.Osipiuk,
C.Hatzos-Skintges,
M.Endres,
C.Y.Chang,
G.Babnigg,
A.Joachimiak,
G.N.Phillips,
B.Shen.
Natural Separation of the Acyl-Coa Ligase Reaction Results in A Non-Adenylating Enzyme. Nat. Chem. Biol. V. 14 730 2018.
Page generated: Sat Dec 12 12:31:48 2020
ISSN: ESSN 1552-4469 PubMed: 29867143 DOI: 10.1038/S41589-018-0061-0 |
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