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Atomistry » Zinc » PDB 4h8p-4hk6 » 4he2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 4h8p-4hk6 » 4he2 » |
Zinc in PDB 4he2: Crystal Structure of Human Muscle Fructose-1,6-Bisphosphatase Q32R Mutant Complex with AmpEnzymatic activity of Crystal Structure of Human Muscle Fructose-1,6-Bisphosphatase Q32R Mutant Complex with Amp
All present enzymatic activity of Crystal Structure of Human Muscle Fructose-1,6-Bisphosphatase Q32R Mutant Complex with Amp:
3.1.3.11; Protein crystallography data
The structure of Crystal Structure of Human Muscle Fructose-1,6-Bisphosphatase Q32R Mutant Complex with Amp, PDB code: 4he2
was solved by
R.Shi,
D.W.Zhu,
S.X.Lin,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4he2:
The structure of Crystal Structure of Human Muscle Fructose-1,6-Bisphosphatase Q32R Mutant Complex with Amp also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Human Muscle Fructose-1,6-Bisphosphatase Q32R Mutant Complex with Amp
(pdb code 4he2). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Human Muscle Fructose-1,6-Bisphosphatase Q32R Mutant Complex with Amp, PDB code: 4he2: Zinc binding site 1 out of 1 in 4he2Go back to Zinc Binding Sites List in 4he2
Zinc binding site 1 out
of 1 in the Crystal Structure of Human Muscle Fructose-1,6-Bisphosphatase Q32R Mutant Complex with Amp
Mono view Stereo pair view
Reference:
R.Shi,
Z.Y.Chen,
D.W.Zhu,
C.Li,
Y.Shan,
G.Xu,
S.X.Lin.
Crystal Structures of Human Muscle Fructose-1,6-Bisphosphatase: Novel Quaternary States, Enhanced Amp Affinity, and Allosteric Signal Transmission Pathway. Plos One V. 8 71242 2013.
Page generated: Sun Oct 27 00:02:13 2024
ISSN: ESSN 1932-6203 PubMed: 24086250 DOI: 10.1371/JOURNAL.PONE.0071242 |
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