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Atomistry » Fluorine » PDB 1mmd-1o5f » 1ney | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Fluorine » PDB 1mmd-1o5f » 1ney » |
Fluorine in PDB 1ney: Triosephosphate Isomerase in Complex with DhapEnzymatic activity of Triosephosphate Isomerase in Complex with Dhap
All present enzymatic activity of Triosephosphate Isomerase in Complex with Dhap:
5.3.1.1; Protein crystallography data
The structure of Triosephosphate Isomerase in Complex with Dhap, PDB code: 1ney
was solved by
G.Jogl,
S.Rozovsky,
A.E.Mcdermott,
L.Tong,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Triosephosphate Isomerase in Complex with Dhap
(pdb code 1ney). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Triosephosphate Isomerase in Complex with Dhap, PDB code: 1ney: Jump to Fluorine binding site number: 1; 2; Fluorine binding site 1 out of 2 in 1neyGo back to Fluorine Binding Sites List in 1ney
Fluorine binding site 1 out
of 2 in the Triosephosphate Isomerase in Complex with Dhap
Mono view Stereo pair view
Fluorine binding site 2 out of 2 in 1neyGo back to Fluorine Binding Sites List in 1ney
Fluorine binding site 2 out
of 2 in the Triosephosphate Isomerase in Complex with Dhap
Mono view Stereo pair view
Reference:
G.Jogl,
S.Rozovsky,
A.E.Mcdermott,
L.Tong.
Optimal Alignment For Enzymatic Proton Transfer: Structure of the Michaelis Complex of Triosephosphate Isomerase at 1.2-A Resolution. Proc.Natl.Acad.Sci.Usa V. 100 50 2003.
Page generated: Sun Dec 13 11:31:17 2020
ISSN: ISSN 0027-8424 PubMed: 12509510 DOI: 10.1073/PNAS.0233793100 |
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