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Atomistry » Molybdenum » PDB 4c80-5koj » 4wn9 » |
Molybdenum in PDB 4wn9: Structure of the Nitrogenase Mofe Protein From Clostridium Pasteurianum Pressurized with XenonEnzymatic activity of Structure of the Nitrogenase Mofe Protein From Clostridium Pasteurianum Pressurized with Xenon
All present enzymatic activity of Structure of the Nitrogenase Mofe Protein From Clostridium Pasteurianum Pressurized with Xenon:
1.18.6.1; Protein crystallography data
The structure of Structure of the Nitrogenase Mofe Protein From Clostridium Pasteurianum Pressurized with Xenon, PDB code: 4wn9
was solved by
C.N.Morrison,
J.A.Hoy,
D.C.Rees,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4wn9:
The structure of Structure of the Nitrogenase Mofe Protein From Clostridium Pasteurianum Pressurized with Xenon also contains other interesting chemical elements:
Molybdenum Binding Sites:
The binding sites of Molybdenum atom in the Structure of the Nitrogenase Mofe Protein From Clostridium Pasteurianum Pressurized with Xenon
(pdb code 4wn9). This binding sites where shown within
5.0 Angstroms radius around Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the Structure of the Nitrogenase Mofe Protein From Clostridium Pasteurianum Pressurized with Xenon, PDB code: 4wn9: Jump to Molybdenum binding site number: 1; 2; Molybdenum binding site 1 out of 2 in 4wn9Go back to![]() ![]()
Molybdenum binding site 1 out
of 2 in the Structure of the Nitrogenase Mofe Protein From Clostridium Pasteurianum Pressurized with Xenon
![]() Mono view ![]() Stereo pair view
Molybdenum binding site 2 out of 2 in 4wn9Go back to![]() ![]()
Molybdenum binding site 2 out
of 2 in the Structure of the Nitrogenase Mofe Protein From Clostridium Pasteurianum Pressurized with Xenon
![]() Mono view ![]() Stereo pair view
Reference:
C.N.Morrison,
J.A.Hoy,
L.Zhang,
O.Einsle,
D.C.Rees.
Substrate Pathways in the Nitrogenase Mofe Protein By Experimental Identification of Small Molecule Binding Sites. Biochemistry 2015.
Page generated: Tue Dec 15 05:19:19 2020
ISSN: ISSN 0006-2960 PubMed: 25710326 DOI: 10.1021/BI501313K |
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