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Iron in PDB 6fxm: Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - Cocrystal with MN2+

Enzymatic activity of Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - Cocrystal with MN2+

All present enzymatic activity of Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - Cocrystal with MN2+:
1.14.11.4;

Protein crystallography data

The structure of Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - Cocrystal with MN2+, PDB code: 6fxm was solved by L.Scietti, A.Chiapparino, F.De Giorgi, M.Fumagalli, L.Khoriauli, S.Nergadze, S.Basu, V.Olieric, B.Banushi, E.Giulotto, P.Gissen, F.Forneris, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.37 / 2.10
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 97.270, 99.949, 225.138, 90.00, 90.00, 90.00
R / Rfree (%) 22.9 / 25.2

Other elements in 6fxm:

The structure of Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - Cocrystal with MN2+ also contains other interesting chemical elements:

Manganese (Mn) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - Cocrystal with MN2+ (pdb code 6fxm). 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 Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - Cocrystal with MN2+, PDB code: 6fxm:

Iron binding site 1 out of 1 in 6fxm

Go back to Iron Binding Sites List in 6fxm
Iron binding site 1 out of 1 in the Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - Cocrystal with MN2+


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - Cocrystal with MN2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe806

b:41.1
occ:1.00
 OD1 A:ASP669 2.0 51.1 1.0
NE2 A:HIS719 2.0 39.2 1.0
NE2 A:HIS667 2.2 46.9 1.0
O5 A:AKG805 2.2 55.9 1.0
O2 A:AKG805 2.3 51.2 1.0
CE1 A:HIS719 2.5 40.7 1.0
CG A:ASP669 2.7 47.7 1.0
OD2 A:ASP669 2.9 54.9 1.0
C2 A:AKG805 2.9 61.8 1.0
C1 A:AKG805 3.0 60.3 1.0
CD2 A:HIS667 3.1 45.6 1.0
CE1 A:HIS667 3.1 45.1 1.0
CD2 A:HIS719 3.3 45.6 1.0
ND1 A:HIS719 3.8 43.2 1.0
CG A:HIS719 4.2 45.9 1.0
ND1 A:HIS667 4.2 47.2 1.0
CB A:ASP669 4.2 40.8 1.0
CG A:HIS667 4.2 47.1 1.0
O1 A:AKG805 4.2 59.8 1.0
O A:HOH1027 4.2 37.1 1.0
NE A:ARG599 4.4 69.9 1.0
CZ A:PHE735 4.4 54.2 1.0
C3 A:AKG805 4.4 57.5 1.0
CE1 A:PHE735 4.5 47.7 1.0
N A:ASP669 4.7 44.0 1.0
CA A:ASP669 4.7 42.0 1.0
CD A:ARG599 4.7 68.6 1.0
C4 A:AKG805 4.9 58.8 1.0
CD2 A:LEU664 4.9 48.8 1.0

Reference:

L.Scietti, A.Chiapparino, F.De Giorgi, M.Fumagalli, L.Khoriauli, S.Nergadze, S.Basu, V.Olieric, L.Cucca, B.Banushi, A.Profumo, E.Giulotto, P.Gissen, F.Forneris. Molecular Architecture of the Multifunctional Collagen Lysyl Hydroxylase and Glycosyltransferase LH3. Nat Commun V. 9 3163 2018.
ISSN: ESSN 2041-1723
PubMed: 30089812
DOI: 10.1038/S41467-018-05631-5
Page generated: Wed Aug 6 06:23:28 2025

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