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Atomistry » Iron » PDB 8ca4-8csp » 8cdf » |
Iron in PDB 8cdf: Structure of Glutarate Hydroxylase (Glah) From Escherichia Coli at A Resolution of 1.8 Angstrom Obtained As A Contaminant During Routine Use of E. Coli As An Expression HostEnzymatic activity of Structure of Glutarate Hydroxylase (Glah) From Escherichia Coli at A Resolution of 1.8 Angstrom Obtained As A Contaminant During Routine Use of E. Coli As An Expression Host
All present enzymatic activity of Structure of Glutarate Hydroxylase (Glah) From Escherichia Coli at A Resolution of 1.8 Angstrom Obtained As A Contaminant During Routine Use of E. Coli As An Expression Host:
1.14.11.64; Protein crystallography data
The structure of Structure of Glutarate Hydroxylase (Glah) From Escherichia Coli at A Resolution of 1.8 Angstrom Obtained As A Contaminant During Routine Use of E. Coli As An Expression Host, PDB code: 8cdf
was solved by
A.A.Adeyeye,
W.Schubert,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Iron Binding Sites:
The binding sites of Iron atom in the Structure of Glutarate Hydroxylase (Glah) From Escherichia Coli at A Resolution of 1.8 Angstrom Obtained As A Contaminant During Routine Use of E. Coli As An Expression Host
(pdb code 8cdf). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Structure of Glutarate Hydroxylase (Glah) From Escherichia Coli at A Resolution of 1.8 Angstrom Obtained As A Contaminant During Routine Use of E. Coli As An Expression Host, PDB code: 8cdf: Iron binding site 1 out of 1 in 8cdfGo back to![]() ![]()
Iron binding site 1 out
of 1 in the Structure of Glutarate Hydroxylase (Glah) From Escherichia Coli at A Resolution of 1.8 Angstrom Obtained As A Contaminant During Routine Use of E. Coli As An Expression Host
![]() Mono view ![]() Stereo pair view
Reference:
A.A.Adeyeye,
W.Schubert.
Structure of Glutarate Hydroxylase (Glah) From Escherichia Coli at A Resolution of 1.8 Angstrom Obtained As A Contaminant During Routine Use of E. Coli As An Expression Host To Be Published.
Page generated: Fri Aug 9 21:14:41 2024
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