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Atomistry » Chlorine » PDB 5jzl-5k92 » 5k3f | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 5jzl-5k92 » 5k3f » |
Chlorine in PDB 5k3f: Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - HIS280ASN/Fluoroacetate - Cocrystallized - Single Protomer Reacted with LigandEnzymatic activity of Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - HIS280ASN/Fluoroacetate - Cocrystallized - Single Protomer Reacted with Ligand
All present enzymatic activity of Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - HIS280ASN/Fluoroacetate - Cocrystallized - Single Protomer Reacted with Ligand:
3.8.1.3; Protein crystallography data
The structure of Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - HIS280ASN/Fluoroacetate - Cocrystallized - Single Protomer Reacted with Ligand, PDB code: 5k3f
was solved by
P.Mehrabi,
T.H.Kim,
S.R.Prosser,
E.F.Pai,
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 Fluoroacetate Dehalogenase RPA1163 - HIS280ASN/Fluoroacetate - Cocrystallized - Single Protomer Reacted with Ligand
(pdb code 5k3f). 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 Fluoroacetate Dehalogenase RPA1163 - HIS280ASN/Fluoroacetate - Cocrystallized - Single Protomer Reacted with Ligand, PDB code: 5k3f: Chlorine binding site 1 out of 1 in 5k3fGo back to Chlorine Binding Sites List in 5k3f
Chlorine binding site 1 out
of 1 in the Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - HIS280ASN/Fluoroacetate - Cocrystallized - Single Protomer Reacted with Ligand
Mono view Stereo pair view
Reference:
T.H.Kim,
P.Mehrabi,
Z.Ren,
A.Sljoka,
C.Ing,
A.Bezginov,
L.Ye,
R.Pomes,
R.S.Prosser,
E.F.Pai.
The Role of Dimer Asymmetry and Protomer Dynamics in Enzyme Catalysis. Science V. 355 2017.
Page generated: Sat Dec 12 11:55:28 2020
ISSN: ESSN 1095-9203 PubMed: 28104837 DOI: 10.1126/SCIENCE.AAG2355 |
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