Zinc in PDB 8pjn: Catalytic Module of Human Ctlh E3 Ligase Bound to Multiphosphorylated UBE2H~Ubiquitin

All present enzymatic activity of Catalytic Module of Human Ctlh E3 Ligase Bound to Multiphosphorylated UBE2H~Ubiquitin:
2.3.2.23; 2.3.2.24; 2.3.2.27;

The binding sites of Zinc atom in the Catalytic Module of Human Ctlh E3 Ligase Bound to Multiphosphorylated UBE2H~Ubiquitin (pdb code 8pjn). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Catalytic Module of Human Ctlh E3 Ligase Bound to Multiphosphorylated UBE2H~Ubiquitin, PDB code: 8pjn:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Catalytic Module of Human Ctlh E3 Ligase Bound to Multiphosphorylated UBE2H~Ubiquitin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Catalytic Module of Human Ctlh E3 Ligase Bound to Multiphosphorylated UBE2H~Ubiquitin within 5.0Å range: probe atom residue distance (Å) B Occ b:Zn501 b:54.2 occ:1.00 ND1 b:HIS356 2.0 35.4 1.0 SG b:CYS354 2.3 38.7 1.0 SG b:CYS374 2.3 43.3 1.0 SG b:CYS377 2.3 44.1 1.0 CE1 b:HIS356 2.8 35.4 1.0 CB b:CYS374 3.1 43.3 1.0 CG b:HIS356 3.1 35.4 1.0 CB b:CYS354 3.3 38.7 1.0 CB b:HIS356 3.7 35.4 1.0 NE2 b:HIS356 3.9 35.4 1.0 CB b:CYS377 4.0 44.1 1.0 CD2 b:HIS356 4.1 35.4 1.0 N b:CYS377 4.1 44.1 1.0 CA b:CYS374 4.5 43.3 1.0 N b:HIS356 4.5 35.4 1.0 O b:CYS377 4.6 44.1 1.0 CA b:CYS377 4.6 44.1 1.0 CD1 b:LEU352 4.6 35.1 1.0 CA b:CYS354 4.7 38.7 1.0 CA b:HIS356 4.7 35.4 1.0 CB b:TYR376 4.9 36.9 1.0

Zinc binding site 2 out of 2 in the Catalytic Module of Human Ctlh E3 Ligase Bound to Multiphosphorylated UBE2H~Ubiquitin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Catalytic Module of Human Ctlh E3 Ligase Bound to Multiphosphorylated UBE2H~Ubiquitin within 5.0Å range: probe atom residue distance (Å) B Occ i:Zn401 b:36.6 occ:1.00 NE2 b:HIS331 2.0 26.7 1.0 SG i:CYS302 2.3 25.7 1.0 SG i:CYS317 2.3 26.4 1.0 SG i:CYS314 2.3 26.0 1.0 CB i:CYS314 2.7 26.0 1.0 CE1 b:HIS331 3.0 26.7 1.0 CD2 b:HIS331 3.0 26.7 1.0 CB i:CYS317 3.7 26.4 1.0 CB i:CYS302 3.8 25.7 1.0 CG1 i:VAL316 4.0 22.1 1.0 N i:CYS317 4.1 26.4 1.0 ND1 b:HIS331 4.1 26.7 1.0 CG b:HIS331 4.2 26.7 1.0 CA i:CYS314 4.2 26.0 1.0 CA i:CYS317 4.3 26.4 1.0 CA i:CYS302 4.4 25.7 1.0 OG i:SER311 4.6 34.7 1.0 CG2 i:THR299 4.6 21.6 1.0 C i:CYS314 4.7 26.0 1.0 C i:VAL316 4.8 22.1 1.0 O i:CYS314 4.8 26.0 1.0 N i:CYS302 4.9 25.7 1.0

J.Chrustowicz, D.Sherpa, J.Li, C.R.Langlois, E.C.Papadopoulou, D.T.Vu, L.A.Hehl, O.Karayel, V.Beier, S.Von Gronau, J.Muller, J.R.Prabu, M.Mann, G.Kleiger, A.F.Alpi, B.A.Schulman. Multisite Phosphorylation Dictates Selective E2-E3 Pairing As Revealed By UBC8/UBE2H-Gid/Ctlh Assemblies. Mol.Cell 2023.
ISSN: ISSN 1097-2765
PubMed: 38113892
DOI: 10.1016/J.MOLCEL.2023.11.027