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Atomistry » Iron » PDB 4dig-4egm » 4dub | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Iron » PDB 4dig-4egm » 4dub » |
Iron in PDB 4dub: Cytochrome P450 BM3H-9D7 Mri Sensor Bound to DopamineEnzymatic activity of Cytochrome P450 BM3H-9D7 Mri Sensor Bound to Dopamine
All present enzymatic activity of Cytochrome P450 BM3H-9D7 Mri Sensor Bound to Dopamine:
1.14.14.1; Protein crystallography data
The structure of Cytochrome P450 BM3H-9D7 Mri Sensor Bound to Dopamine, PDB code: 4dub
was solved by
E.M.Brustad,
V.S.Lelyveld,
C.D.Snow,
N.Crook,
F.M.Martinez,
T.J.Scholl,
A.Jasanoff,
F.H.Arnold,
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 Cytochrome P450 BM3H-9D7 Mri Sensor Bound to Dopamine
(pdb code 4dub). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Cytochrome P450 BM3H-9D7 Mri Sensor Bound to Dopamine, PDB code: 4dub: Jump to Iron binding site number: 1; 2; Iron binding site 1 out of 2 in 4dubGo back to Iron Binding Sites List in 4dub
Iron binding site 1 out
of 2 in the Cytochrome P450 BM3H-9D7 Mri Sensor Bound to Dopamine
Mono view Stereo pair view
Iron binding site 2 out of 2 in 4dubGo back to Iron Binding Sites List in 4dub
Iron binding site 2 out
of 2 in the Cytochrome P450 BM3H-9D7 Mri Sensor Bound to Dopamine
Mono view Stereo pair view
Reference:
E.M.Brustad,
V.S.Lelyveld,
C.D.Snow,
N.Crook,
S.T.Jung,
F.M.Martinez,
T.J.Scholl,
A.Jasanoff,
F.H.Arnold.
Structure-Guided Directed Evolution of Highly Selective P450-Based Magnetic Resonance Imaging Sensors For Dopamine and Serotonin. J.Mol.Biol. V. 422 245 2012.
Page generated: Sun Dec 13 15:32:18 2020
ISSN: ISSN 0022-2836 PubMed: 22659321 DOI: 10.1016/J.JMB.2012.05.029 |
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