Iron in PDB 6teu: Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - VAL80LYS Mutant - Cocrystal with FE2+, MN2+

All present enzymatic activity of Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - VAL80LYS Mutant - Cocrystal with FE2+, MN2+:
1.14.11.4; 2.4.1.50; 2.4.1.66;

The structure of Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - VAL80LYS Mutant - Cocrystal with FE2+, MN2+, PDB code: 6teu 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)	49.14 / 3.00
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	98.004, 100.691, 225.674, 90, 90, 90
R / Rfree (%)	20.8 / 24.1

The structure of Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - VAL80LYS Mutant - Cocrystal with FE2+, MN2+ 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 - VAL80LYS Mutant - Cocrystal with FE2+, MN2+ (pdb code 6teu). 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 - VAL80LYS Mutant - Cocrystal with FE2+, MN2+, PDB code: 6teu:
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 - VAL80LYS Mutant - Cocrystal with FE2+, 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 - VAL80LYS Mutant - Cocrystal with FE2+, MN2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe804 b:32.1 occ:1.00 OD1 A:ASP669 2.4 59.0 1.0 NE2 A:HIS719 2.5 35.2 1.0 C1 A:AKG803 2.6 42.3 1.0 OD2 A:ASP669 2.6 59.9 1.0 NE2 A:HIS667 2.7 57.7 1.0 O2 A:AKG803 2.7 45.6 1.0 CG A:ASP669 2.8 57.9 1.0 O5 A:AKG803 2.8 22.1 1.0 C2 A:AKG803 2.9 34.3 1.0 O1 A:AKG803 3.1 42.6 1.0 CD2 A:HIS667 3.2 57.5 1.0 CD2 A:HIS719 3.3 35.3 1.0 CE1 A:HIS719 3.6 36.9 1.0 CE1 A:PHE735 3.7 25.4 1.0 CE1 A:HIS667 3.7 60.0 1.0 CZ A:PHE735 3.9 26.5 1.0 CB A:ASP669 4.2 54.5 1.0 C3 A:AKG803 4.3 39.3 1.0 CG A:HIS667 4.4 56.6 1.0 CG A:HIS719 4.5 35.0 1.0 O A:HIS668 4.6 59.3 1.0 NE A:ARG599 4.6 54.3 1.0 ND1 A:HIS667 4.6 57.7 1.0 ND1 A:HIS719 4.7 36.1 1.0 CG2 A:THR674 4.7 35.6 1.0 CA A:ASP669 4.7 50.0 1.0 CD1 A:PHE735 4.8 26.2 1.0 C A:HIS668 4.9 54.8 1.0 N A:ASP669 5.0 52.1 1.0 NE2 A:HIS711 5.0 40.7 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - VAL80LYS Mutant - Cocrystal with FE2+, MN2+


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 - VAL80LYS Mutant - Cocrystal with FE2+, MN2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe805 b:47.7 occ:1.00 OD2 A:ASP611 2.6 29.4 1.0 NE2 A:HIS595 2.6 108.2 1.0 OD2 A:ASP597 2.6 87.6 1.0 CE1 A:HIS613 2.7 34.8 1.0 OD1 A:ASP611 2.8 27.7 1.0 CG A:ASP611 2.9 29.1 1.0 CE1 A:HIS595 3.0 108.3 1.0 CG A:ASP597 3.2 87.3 1.0 OD1 A:ASP597 3.5 86.7 1.0 ND1 A:HIS613 3.6 35.0 1.0 NE2 A:HIS613 3.7 35.7 1.0 CD2 A:HIS595 3.9 108.8 1.0 CB A:ASP611 4.1 32.9 1.0 CB A:ASP597 4.2 87.2 1.0 ND1 A:HIS595 4.3 109.2 1.0 CD2 A:PHE652 4.3 40.0 1.0 CG A:PHE652 4.4 41.3 1.0 O A:GLU596 4.4 96.9 1.0 CE2 A:PHE652 4.6 39.0 1.0 CA A:ASP597 4.7 88.6 1.0 CD1 A:PHE652 4.7 39.2 1.0 CG A:HIS595 4.7 109.2 1.0 CB A:PHE652 4.8 42.0 1.0 CG A:HIS613 4.8 36.7 1.0 CD2 A:HIS613 4.9 35.9 1.0 CZ A:PHE652 4.9 38.7 1.0 NH1 A:ARG599 5.0 55.9 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.