Zinc in PDB 8ost: Structure of Human Terminal Uridylyltransferase 4 (TUT4, ZCCHC11) in Complex with Pre-LET7G Mirna and LIN28A

All present enzymatic activity of Structure of Human Terminal Uridylyltransferase 4 (TUT4, ZCCHC11) in Complex with Pre-LET7G Mirna and LIN28A:
2.7.7.52;

The binding sites of Zinc atom in the Structure of Human Terminal Uridylyltransferase 4 (TUT4, ZCCHC11) in Complex with Pre-LET7G Mirna and LIN28A (pdb code 8ost). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Human Terminal Uridylyltransferase 4 (TUT4, ZCCHC11) in Complex with Pre-LET7G Mirna and LIN28A, PDB code: 8ost:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of Human Terminal Uridylyltransferase 4 (TUT4, ZCCHC11) in Complex with Pre-LET7G Mirna and LIN28A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Human Terminal Uridylyltransferase 4 (TUT4, ZCCHC11) in Complex with Pre-LET7G Mirna and LIN28A within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn301 b:110.7 occ:1.00 HE1 B:HIS147 1.4 95.0 1.0 CE1 B:HIS147 1.9 95.0 1.0 ND1 B:HIS147 2.2 95.0 1.0 HG B:CYS152 2.2 97.0 1.0 SG B:CYS139 2.3 95.5 1.0 SG B:CYS152 2.3 97.0 1.0 SG B:CYS142 2.3 97.8 1.0 HB2 B:CYS152 2.5 97.0 1.0 HG B:CYS142 2.6 97.8 1.0 CB B:CYS152 2.9 97.0 1.0 HB3 B:CYS139 3.1 95.5 1.0 CB B:CYS139 3.1 95.5 1.0 HB2 B:CYS139 3.1 95.5 1.0 NE2 B:HIS147 3.2 95.0 1.0 CG B:HIS147 3.5 95.0 1.0 HB3 B:CYS142 3.5 97.8 1.0 O B:HIS147 3.6 95.0 1.0 H B:CYS142 3.6 97.8 1.0 CB B:CYS142 3.6 97.8 1.0 HB3 B:CYS152 3.6 97.0 1.0 HA B:CYS152 3.7 97.0 1.0 HE2 B:HIS147 3.7 95.0 1.0 CA B:CYS152 3.9 97.0 1.0 CD2 B:HIS147 4.0 95.0 1.0 HB3 B:ASN141 4.1 92.7 1.0 H B:GLY144 4.2 101.0 1.0 N B:CYS142 4.2 97.8 1.0 O B:HIS148 4.3 95.2 1.0 C B:HIS147 4.3 95.0 1.0 HB2 B:CYS142 4.3 97.8 1.0 HG B:LEU154 4.4 96.2 1.0 HA B:ALA149 4.4 88.9 1.0 H B:HIS147 4.5 95.0 1.0 CA B:CYS142 4.5 97.8 1.0 HD21 B:ASN141 4.5 92.7 1.0 OD1 B:ASP146 4.5 98.5 1.0 O B:GLY144 4.6 101.0 1.0 CA B:CYS139 4.6 95.5 1.0 CB B:HIS147 4.6 95.0 1.0 H B:CYS152 4.7 97.0 1.0 C B:HIS148 4.7 95.2 1.0 HB2 B:HIS147 4.7 95.0 1.0 HD21 B:LEU154 4.7 96.2 1.0 N B:CYS152 4.8 97.0 1.0 H B:ASN141 4.8 92.7 1.0 HA B:CYS139 4.8 95.5 1.0 HA3 B:GLY144 4.9 101.0 1.0 CA B:HIS147 4.9 95.0 1.0 H B:GLY143 4.9 103.1 1.0 HD2 B:HIS147 4.9 95.0 1.0 N B:GLY144 5.0 101.0 1.0

Zinc binding site 2 out of 2 in the Structure of Human Terminal Uridylyltransferase 4 (TUT4, ZCCHC11) in Complex with Pre-LET7G Mirna and LIN28A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Human Terminal Uridylyltransferase 4 (TUT4, ZCCHC11) in Complex with Pre-LET7G Mirna and LIN28A within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn302 b:156.4 occ:1.00 HG B:CYS161 1.3 127.8 1.0 SG B:CYS164 2.3 131.3 1.0 SG B:CYS161 2.3 127.8 1.0 SG B:CYS174 2.3 133.6 1.0 HG B:CYS164 2.5 131.3 1.0 HG B:CYS174 2.6 133.6 1.0 HB3 B:CYS164 2.6 131.3 1.0 HB2 B:CYS174 2.6 133.6 1.0 CB B:CYS174 2.9 133.6 1.0 H B:CYS164 2.9 131.3 1.0 CB B:CYS164 3.0 131.3 1.0 HA B:CYS174 3.2 133.6 1.0 HB2 B:PHE163 3.2 126.2 1.0 N B:CYS164 3.4 131.3 1.0 HD2 B:HIS169 3.4 129.3 1.0 CA B:CYS174 3.6 133.6 1.0 CB B:CYS161 3.6 127.8 1.0 HB3 B:CYS161 3.7 127.8 1.0 HE2 B:HIS169 3.7 129.3 1.0 HD2 B:PRO175 3.7 135.9 1.0 HB2 B:CYS164 3.8 131.3 1.0 HB3 B:CYS174 3.8 133.6 1.0 CA B:CYS164 3.8 131.3 1.0 HG B:SER166 3.9 126.2 1.0 HB2 B:CYS161 3.9 127.8 1.0 CD2 B:HIS169 3.9 129.3 1.0 HA B:VAL171 4.0 128.8 1.0 CB B:PHE163 4.0 126.2 1.0 NE2 B:HIS169 4.1 129.3 1.0 HB3 B:PHE163 4.1 126.2 1.0 C B:PHE163 4.3 126.2 1.0 O B:MET170 4.3 130.9 1.0 H B:PHE163 4.4 126.2 1.0 HA B:CYS164 4.5 131.3 1.0 CD B:PRO175 4.5 135.9 1.0 N B:CYS174 4.6 133.6 1.0 OG B:SER166 4.6 126.2 1.0 CA B:PHE163 4.6 126.2 1.0 H B:CYS174 4.7 133.6 1.0 C B:CYS164 4.7 131.3 1.0 HD3 B:PRO175 4.7 135.9 1.0 N B:PHE163 4.7 126.2 1.0 C B:CYS174 4.7 133.6 1.0 H B:GLN165 4.8 126.8 1.0 H B:SER166 4.9 126.2 1.0 CA B:VAL171 4.9 128.8 1.0 CA B:CYS161 4.9 127.8 1.0 N B:PRO175 5.0 135.9 1.0

G.Ye, M.Yi, L.Carrique, A.El-Sagheer, T.Brown, C.J.Norbury, P.Zhang, R.J.Gilbert. Structural Basis For Activity Switching in Polymerases Determining the Fate of Let-7 Pre-Mirnas To Be Published.