Iron in PDB 8zgc: Human Lysine O-Link Glycosylation Complex, LH3/COLGALT1 with Bound Udp-Galactose

All present enzymatic activity of Human Lysine O-Link Glycosylation Complex, LH3/COLGALT1 with Bound Udp-Galactose:
1.14.11.4; 2.4.1.50; 2.4.1.66;

The structure of Human Lysine O-Link Glycosylation Complex, LH3/COLGALT1 with Bound Udp-Galactose also contains other interesting chemical elements:

Manganese

(Mn)

6 atoms

The binding sites of Iron atom in the Human Lysine O-Link Glycosylation Complex, LH3/COLGALT1 with Bound Udp-Galactose (pdb code 8zgc). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Human Lysine O-Link Glycosylation Complex, LH3/COLGALT1 with Bound Udp-Galactose, PDB code: 8zgc:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Human Lysine O-Link Glycosylation Complex, LH3/COLGALT1 with Bound Udp-Galactose


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Human Lysine O-Link Glycosylation Complex, LH3/COLGALT1 with Bound Udp-Galactose within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe804 b:88.2 occ:1.00 O5 A:AKG803 2.5 86.1 1.0 OD1 A:ASP669 2.5 73.8 1.0 C2 A:AKG803 2.5 86.1 1.0 OD2 A:ASP669 2.6 73.8 1.0 O2 A:AKG803 2.7 86.1 1.0 CG A:ASP669 2.8 73.8 1.0 C1 A:AKG803 2.9 86.1 1.0 NE2 A:HIS719 2.9 74.1 1.0 C4 A:AKG803 3.2 86.1 1.0 C3 A:AKG803 3.3 86.1 1.0 CE1 A:HIS719 3.3 74.1 1.0 NE2 A:HIS667 3.6 73.5 1.0 O1 A:AKG803 4.0 86.1 1.0 CD2 A:HIS719 4.0 74.1 1.0 CB A:ASP669 4.2 73.8 1.0 CE1 A:HIS667 4.2 73.5 1.0 C5 A:AKG803 4.3 86.1 1.0 CE1 A:PHE735 4.4 71.5 1.0 ND1 A:HIS719 4.4 74.1 1.0 CZ A:PHE735 4.5 71.5 1.0 O3 A:AKG803 4.5 86.1 1.0 CD2 A:HIS667 4.6 73.5 1.0 CG A:HIS719 4.8 74.1 1.0 CG2 A:THR674 4.8 76.4 1.0 OG1 A:THR674 4.9 76.4 1.0

Iron binding site 2 out of 2 in the Human Lysine O-Link Glycosylation Complex, LH3/COLGALT1 with Bound Udp-Galactose


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Human Lysine O-Link Glycosylation Complex, LH3/COLGALT1 with Bound Udp-Galactose within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe804 b:67.9 occ:1.00 NE2 B:HIS719 2.3 49.6 1.0 OD1 B:ASP669 2.6 52.1 1.0 OD2 B:ASP669 2.7 52.1 1.0 O5 B:AKG803 2.7 58.4 1.0 CE1 B:HIS719 2.8 49.6 1.0 CG B:ASP669 3.0 52.1 1.0 O2 B:AKG803 3.3 58.4 1.0 NE2 B:HIS667 3.4 52.8 1.0 C2 B:AKG803 3.6 58.4 1.0 CD2 B:HIS719 3.6 49.6 1.0 C1 B:AKG803 3.9 58.4 1.0 CE1 B:HIS667 4.0 52.8 1.0 ND1 B:HIS719 4.1 49.6 1.0 CD2 B:HIS667 4.4 52.8 1.0 CB B:ASP669 4.4 52.1 1.0 CG B:HIS719 4.5 49.6 1.0 CE1 B:PHE735 4.7 52.7 1.0 CZ B:PHE735 4.9 52.7 1.0 C3 B:AKG803 4.9 58.4 1.0 OG1 B:THR674 4.9 39.5 1.0 CG2 B:THR674 5.0 39.5 1.0 CE1 B:HIS711 5.0 40.0 1.0

J.Peng, W.Li, D.Yao, Y.Xia, Q.Wang, Y.Cai, S.Li, M.Cao, Y.Shen, P.Ma, R.Liao, J.Zhao, A.Qin, Y.Cao. The Structural Basis For the Human Procollagen Lysine Hydroxylation and Dual-Glycosylation. Nat Commun 2025.
ISSN: ESSN 2041-1723
DOI: 10.1038/S41467-025-57768-9