Zinc in PDB 8ops: Human Terminal Uridylyltransferase 7 (TUT7/ZCCHC6) Bound with Pre- LET7G Mirna and LIN28A - Complex 1

Enzymatic activity of Human Terminal Uridylyltransferase 7 (TUT7/ZCCHC6) Bound with Pre- LET7G Mirna and LIN28A - Complex 1

All present enzymatic activity of Human Terminal Uridylyltransferase 7 (TUT7/ZCCHC6) Bound with Pre- LET7G Mirna and LIN28A - Complex 1:
2.7.7.52;

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Terminal Uridylyltransferase 7 (TUT7/ZCCHC6) Bound with Pre- LET7G Mirna and LIN28A - Complex 1 (pdb code 8ops). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Human Terminal Uridylyltransferase 7 (TUT7/ZCCHC6) Bound with Pre- LET7G Mirna and LIN28A - Complex 1, PDB code: 8ops:

Zinc binding site 1 out of 1 in 8ops

Go back to Zinc Binding Sites List in 8ops
Zinc binding site 1 out of 1 in the Human Terminal Uridylyltransferase 7 (TUT7/ZCCHC6) Bound with Pre- LET7G Mirna and LIN28A - Complex 1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Terminal Uridylyltransferase 7 (TUT7/ZCCHC6) Bound with Pre- LET7G Mirna and LIN28A - Complex 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn301

b:161.5
occ:1.00
O B:ASN141 2.0 123.8 1.0
SG B:CYS142 2.3 133.4 1.0
SG B:CYS152 2.3 129.4 1.0
SG B:CYS139 2.3 130.1 1.0
HB3 B:CYS139 2.8 130.1 1.0
CB B:CYS139 3.1 130.1 1.0
C B:ASN141 3.2 123.8 1.0
H B:GLY144 3.2 136.6 1.0
HA B:ALA149 3.3 129.5 1.0
HB2 B:CYS139 3.5 130.1 1.0
H B:ASN141 3.6 123.8 1.0
CB B:CYS152 3.6 129.4 1.0
HB2 B:CYS152 3.7 129.4 1.0
CB B:CYS142 3.8 133.4 1.0
HB3 B:CYS152 3.8 129.4 1.0
HB2 B:HIS147 3.8 128.7 1.0
H B:GLY143 4.0 132.1 1.0
N B:GLY144 4.0 136.6 1.0
N B:CYS142 4.0 133.4 1.0
HB3 B:CYS142 4.1 133.4 1.0
N B:ASN141 4.1 123.8 1.0
CA B:ASN141 4.2 123.8 1.0
O B:HIS148 4.2 126.4 1.0
HB3 B:ASN141 4.2 123.8 1.0
HA3 B:GLY144 4.2 136.6 1.0
CA B:ALA149 4.2 129.5 1.0
CA B:CYS142 4.2 133.4 1.0
N B:GLY143 4.2 132.1 1.0
O B:HIS147 4.3 128.7 1.0
C B:CYS142 4.3 133.4 1.0
C B:HIS148 4.4 126.4 1.0
CA B:CYS139 4.5 130.1 1.0
HB2 B:CYS142 4.5 133.4 1.0
N B:ALA149 4.5 129.5 1.0
O B:GLY144 4.6 136.6 1.0
CA B:GLY144 4.6 136.6 1.0
CB B:ASN141 4.6 123.8 1.0
OD1 B:ASN141 4.6 123.8 1.0
C B:CYS139 4.7 130.1 1.0
CB B:HIS147 4.7 128.7 1.0
HB3 B:ALA149 4.8 129.5 1.0
HB3 B:HIS147 4.8 128.7 1.0
C B:HIS147 4.8 128.7 1.0
H B:CYS142 4.8 133.4 1.0
H B:CYS152 4.9 129.4 1.0
H B:TYR140 4.9 126.7 1.0
CG B:ASN141 4.9 123.8 1.0
N B:TYR140 4.9 126.7 1.0
CA B:CYS152 5.0 129.4 1.0
CB B:ALA149 5.0 129.5 1.0
HA B:ASN141 5.0 123.8 1.0

Reference:

G.Yi, M.Ye, L.Carrique, A.El-Sagheer, T.Brown, C.J.Norbury, P.Zhang, R.J.C.Gilbert. Structural Basis For Activity Switching in Polymerases Determining the Fate of Let-7 Pre-Mirnas Nat.Struct.Mol.Biol. 2024.
ISSN: ESSN 1545-9985
DOI: 10.1038/S41594-024-01357-9
Page generated: Thu Oct 31 08:52:35 2024

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