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Manganese in PDB 8one: Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - ASP190SER Mutant - Cocrystal with FE2+, MN2+, Udp-GlucoseEnzymatic activity of Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - ASP190SER Mutant - Cocrystal with FE2+, MN2+, Udp-Glucose
All present enzymatic activity of Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - ASP190SER Mutant - Cocrystal with FE2+, MN2+, Udp-Glucose:
1.14.11.4; 2.4.1.50; 2.4.1.66; Protein crystallography data
The structure of Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - ASP190SER Mutant - Cocrystal with FE2+, MN2+, Udp-Glucose, PDB code: 8one
was solved by
D.Mattoteia,
M.De Marco,
A.Pinnola,
S.Faravelli,
L.Scietti,
F.Forneris,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 8one:
The structure of Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - ASP190SER Mutant - Cocrystal with FE2+, MN2+, Udp-Glucose also contains other interesting chemical elements:
Manganese Binding Sites:
The binding sites of Manganese atom in the Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - ASP190SER Mutant - Cocrystal with FE2+, MN2+, Udp-Glucose
(pdb code 8one). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - ASP190SER Mutant - Cocrystal with FE2+, MN2+, Udp-Glucose, PDB code: 8one: Manganese binding site 1 out of 1 in 8oneGo back to Manganese Binding Sites List in 8one
Manganese binding site 1 out
of 1 in the Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - ASP190SER Mutant - Cocrystal with FE2+, MN2+, Udp-Glucose
Mono view Stereo pair view
Reference:
D.Mattoteia,
A.Chiapparino,
M.Fumagalli,
M.De Marco,
F.De Giorgi,
L.Negro,
A.Pinnola,
S.Faravelli,
T.Roscioli,
L.Scietti,
F.Forneris.
Identification of Regulatory Molecular 'Hot Spots' For Lh/Plod Collagen Glycosyltransferase Activity Int J Mol Sci 2023.
Page generated: Fri Jul 28 02:20:58 2023
ISSN: ESSN 1422-0067 DOI: 10.3390/IJMS241311213 |
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