Iron in PDB 6tec: Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - Cocrystal with FE2+, MN2+, Udp-Xylose

All present enzymatic activity of Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - Cocrystal with FE2+, MN2+, Udp-Xylose:
1.14.11.4; 2.4.1.50; 2.4.1.66;

The structure of Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - Cocrystal with FE2+, MN2+, Udp-Xylose, PDB code: 6tec was solved by A.Chiapparino, F.De Giorgi, L.Scietti, S.Faravelli, T.Roscioli, F.Forneris, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.79 / 2.40
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	97.264, 99.987, 223.96, 90, 90, 90
R / Rfree (%)	18.5 / 21.6

The structure of Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - Cocrystal with FE2+, MN2+, Udp-Xylose also contains other interesting chemical elements:

Manganese

(Mn)

1 atom

The binding sites of Iron atom in the Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - Cocrystal with FE2+, MN2+, Udp-Xylose (pdb code 6tec). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - Cocrystal with FE2+, MN2+, Udp-Xylose, PDB code: 6tec:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - Cocrystal with FE2+, MN2+, Udp-Xylose


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 FE2+, MN2+, Udp-Xylose within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe803 b:19.3 occ:1.00 OD1 A:ASP669 2.5 22.0 1.0 NE2 A:HIS719 2.5 19.0 1.0 O2 A:AKG802 2.5 49.4 1.0 O5 A:AKG802 2.5 61.0 1.0 NE2 A:HIS667 2.5 33.4 1.0 OD2 A:ASP669 2.7 21.4 1.0 CG A:ASP669 2.9 27.1 1.0 C1 A:AKG802 2.9 53.2 1.0 C2 A:AKG802 3.1 58.7 1.0 CD2 A:HIS719 3.3 20.2 1.0 CD2 A:HIS667 3.4 32.0 1.0 CE1 A:HIS719 3.5 27.0 1.0 CE1 A:HIS667 3.5 33.9 1.0 O1 A:AKG802 3.9 54.0 1.0 CE1 A:PHE735 4.2 24.6 1.0 NE A:ARG599 4.3 29.1 1.0 CZ A:PHE735 4.3 23.8 1.0 CB A:ASP669 4.4 30.5 1.0 CG A:HIS719 4.5 25.8 1.0 CG A:HIS667 4.5 33.0 1.0 C3 A:AKG802 4.6 58.7 1.0 ND1 A:HIS719 4.6 27.9 1.0 ND1 A:HIS667 4.6 32.6 1.0 CD A:ARG599 4.7 30.8 1.0 CD2 A:LEU664 4.9 21.3 1.0 CG2 A:THR674 5.0 23.4 1.0 CE1 A:HIS711 5.0 22.5 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - Cocrystal with FE2+, MN2+, Udp-Xylose


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - Cocrystal with FE2+, MN2+, Udp-Xylose within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe804 b:23.5 occ:1.00 NE2 A:HIS595 2.5 60.4 1.0 OD1 A:ASP597 2.5 52.0 1.0 NE2 A:HIS613 2.6 33.6 1.0 OD2 A:ASP611 2.6 26.7 1.0 OD1 A:ASP611 2.6 24.3 1.0 OD2 A:ASP597 2.7 49.9 1.0 CG A:ASP611 2.9 29.2 1.0 CG A:ASP597 2.9 52.4 1.0 CD2 A:HIS613 3.3 32.6 1.0 CE1 A:HIS595 3.4 60.3 1.0 CD2 A:HIS595 3.5 62.5 1.0 CE1 A:HIS613 3.7 35.0 1.0 OG1 A:THR609 4.2 33.4 1.0 CB A:ASP611 4.3 33.8 1.0 CB A:ASP597 4.3 55.0 1.0 O A:GLU596 4.4 55.6 1.0 O A:THR609 4.4 35.9 1.0 CG A:PHE652 4.5 24.1 1.0 ND1 A:HIS595 4.5 63.1 1.0 CG A:HIS613 4.5 32.0 1.0 CG A:HIS595 4.6 64.3 1.0 CD2 A:PHE652 4.6 24.4 1.0 CD1 A:PHE652 4.7 25.7 1.0 CA A:ASP597 4.7 55.0 1.0 ND1 A:HIS613 4.7 34.4 1.0 CB A:PHE652 4.8 22.7 1.0 OG A:SER591 4.9 36.8 1.0 CE2 A:PHE652 4.9 24.6 1.0 C A:GLU596 5.0 55.6 1.0 CE1 A:PHE652 5.0 21.3 1.0

A.Chiapparino, F.De Giorgi, L.Scietti, S.Faravelli, T.Roscioli, F.Forneris. A Cooperative Network of Molecular "Hot Spots" Highlights the Complexity of LH3 Collagen Glycosyltransferase Activities To Be Published.