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Calcium in PDB 7jvl: Structure of the M101A Variant of the Sida Ornithine Hydroxylase Complexed with Nadp and the Fad in the "Out" ConformationEnzymatic activity of Structure of the M101A Variant of the Sida Ornithine Hydroxylase Complexed with Nadp and the Fad in the "Out" Conformation
All present enzymatic activity of Structure of the M101A Variant of the Sida Ornithine Hydroxylase Complexed with Nadp and the Fad in the "Out" Conformation:
1.14.13.196; Protein crystallography data
The structure of Structure of the M101A Variant of the Sida Ornithine Hydroxylase Complexed with Nadp and the Fad in the "Out" Conformation, PDB code: 7jvl
was solved by
J.J.Tanner,
A.C.Campbell,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Calcium Binding Sites:
The binding sites of Calcium atom in the Structure of the M101A Variant of the Sida Ornithine Hydroxylase Complexed with Nadp and the Fad in the "Out" Conformation
(pdb code 7jvl). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Structure of the M101A Variant of the Sida Ornithine Hydroxylase Complexed with Nadp and the Fad in the "Out" Conformation, PDB code: 7jvl: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 7jvlGo back to Calcium Binding Sites List in 7jvl
Calcium binding site 1 out
of 2 in the Structure of the M101A Variant of the Sida Ornithine Hydroxylase Complexed with Nadp and the Fad in the "Out" Conformation
Mono view Stereo pair view
Calcium binding site 2 out of 2 in 7jvlGo back to Calcium Binding Sites List in 7jvl
Calcium binding site 2 out
of 2 in the Structure of the M101A Variant of the Sida Ornithine Hydroxylase Complexed with Nadp and the Fad in the "Out" Conformation
Mono view Stereo pair view
Reference:
A.C.Campbell,
R.Robinson,
D.Mena-Aguilar,
P.Sobrado,
J.J.Tanner.
Structural Determinants of Flavin Dynamics in A Class B Monooxygenase. Biochemistry 2020.
Page generated: Sat Dec 12 08:07:13 2020
ISSN: ISSN 0006-2960 PubMed: 33226785 DOI: 10.1021/ACS.BIOCHEM.0C00783 |
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