Iron in PDB 6te3: Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - Cocrystal with FE2+, MN2+, Udp

All present enzymatic activity of Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - Cocrystal with FE2+, MN2+, Udp:
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, PDB code: 6te3 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)	48.84 / 2.30
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	96.995, 100.035, 225.208, 90, 90, 90
R / Rfree (%)	19.4 / 24.6

The structure of Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - Cocrystal with FE2+, MN2+, Udp 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 (pdb code 6te3). 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, PDB code: 6te3:
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


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe805 b:35.2 occ:1.00 OD1 A:ASP669 2.3 42.8 1.0 O2 A:AKG804 2.4 35.9 1.0 O5 A:AKG804 2.4 37.4 1.0 CE1 A:HIS719 2.5 28.6 1.0 NE2 A:HIS719 2.6 34.5 1.0 NE2 A:HIS667 2.7 29.0 1.0 OD2 A:ASP669 2.9 33.8 1.0 C1 A:AKG804 2.9 38.9 1.0 CG A:ASP669 2.9 38.2 1.0 C2 A:AKG804 3.0 45.8 1.0 CD2 A:HIS667 3.3 30.1 1.0 ND1 A:HIS719 3.8 29.4 1.0 CE1 A:HIS667 3.8 31.8 1.0 CZ A:PHE735 3.8 34.4 1.0 CE1 A:PHE735 3.9 32.1 1.0 CD2 A:HIS719 4.0 34.8 1.0 O1 A:AKG804 4.0 36.3 1.0 NE A:ARG599 4.1 41.1 1.0 CB A:ASP669 4.3 39.3 1.0 C3 A:AKG804 4.5 50.4 1.0 CD A:ARG599 4.5 44.2 1.0 CG A:HIS719 4.5 32.4 1.0 CG A:HIS667 4.6 30.5 1.0 O A:HIS668 4.7 42.9 1.0 CA A:ASP669 4.8 33.3 1.0 ND1 A:HIS667 4.8 29.8 1.0 CG A:ARG599 4.8 46.3 1.0 C A:HIS668 5.0 37.0 1.0 CE2 A:PHE735 5.0 36.7 1.0 N A:ASP669 5.0 35.6 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


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe806 b:57.5 occ:1.00 NE2 A:HIS595 2.5 101.3 1.0 OD2 A:ASP611 2.6 42.8 1.0 OD1 A:ASP611 2.6 41.8 1.0 OD1 A:ASP597 2.7 86.5 1.0 NE2 A:HIS613 2.7 28.5 1.0 CG A:ASP611 2.8 42.6 1.0 OD2 A:ASP597 2.9 87.8 1.0 CE1 A:HIS595 3.1 101.2 1.0 CG A:ASP597 3.1 87.3 1.0 CD2 A:HIS613 3.4 28.1 1.0 CD2 A:HIS595 3.6 102.6 1.0 CE1 A:HIS613 3.7 30.1 1.0 CB A:ASP611 4.1 39.0 1.0 CD2 A:PHE652 4.3 22.2 1.0 ND1 A:HIS595 4.3 102.8 1.0 CG A:PHE652 4.3 25.1 1.0 O A:GLU596 4.4 99.3 1.0 OG1 A:THR609 4.4 40.3 1.0 CB A:ASP597 4.6 91.0 1.0 CG A:HIS613 4.6 30.6 1.0 CG A:HIS595 4.6 103.5 1.0 CB A:PHE652 4.6 26.6 1.0 CD1 A:PHE652 4.7 24.8 1.0 CE2 A:PHE652 4.7 17.6 1.0 ND1 A:HIS613 4.7 30.3 1.0 O A:THR609 4.9 36.9 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.