Zinc in PDB 9dj8: Rna-NSP9 Bound to the Niran Domain of the E-Rtc with An Empty G-Pocket
Enzymatic activity of Rna-NSP9 Bound to the Niran Domain of the E-Rtc with An Empty G-Pocket
All present enzymatic activity of Rna-NSP9 Bound to the Niran Domain of the E-Rtc with An Empty G-Pocket:
2.7.7.48;
Zinc Binding Sites:
The binding sites of Zinc atom in the Rna-NSP9 Bound to the Niran Domain of the E-Rtc with An Empty G-Pocket
(pdb code 9dj8). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the
Rna-NSP9 Bound to the Niran Domain of the E-Rtc with An Empty G-Pocket, PDB code: 9dj8:
Jump to Zinc binding site number:
1;
2;
Zinc binding site 1 out
of 2 in 9dj8
Go back to
Zinc Binding Sites List in 9dj8
Zinc binding site 1 out
of 2 in the Rna-NSP9 Bound to the Niran Domain of the E-Rtc with An Empty G-Pocket
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Rna-NSP9 Bound to the Niran Domain of the E-Rtc with An Empty G-Pocket within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1001
b:25.8
occ:1.00
|
ND1
|
A:HIS295
|
2.3
|
0.9
|
1.0
|
SG
|
A:CYS301
|
2.3
|
1.3
|
1.0
|
SG
|
A:CYS310
|
2.4
|
2.0
|
1.0
|
SG
|
A:CYS306
|
2.4
|
6.1
|
1.0
|
HB2
|
A:HIS295
|
3.1
|
0.5
|
1.0
|
CE1
|
A:HIS295
|
3.2
|
0.7
|
1.0
|
HE1
|
A:HIS295
|
3.3
|
0.7
|
1.0
|
CG
|
A:HIS295
|
3.4
|
0.6
|
1.0
|
HA
|
A:CYS301
|
3.4
|
1.6
|
1.0
|
O
|
A:CYS306
|
3.4
|
1.4
|
1.0
|
HB2
|
A:CYS310
|
3.5
|
1.0
|
1.0
|
CB
|
A:CYS301
|
3.5
|
1.8
|
1.0
|
HB3
|
A:CYS301
|
3.6
|
2.0
|
1.0
|
CB
|
A:CYS310
|
3.6
|
0.9
|
1.0
|
H
|
A:HIS295
|
3.6
|
0.5
|
1.0
|
CB
|
A:HIS295
|
3.7
|
0.6
|
1.0
|
CB
|
A:CYS306
|
3.8
|
1.9
|
1.0
|
C
|
A:CYS306
|
3.9
|
1.2
|
1.0
|
HB3
|
A:CYS306
|
3.9
|
2.3
|
1.0
|
CA
|
A:CYS301
|
4.0
|
1.6
|
1.0
|
HD1
|
A:HIS309
|
4.0
|
0.3
|
1.0
|
HB3
|
A:CYS310
|
4.1
|
0.7
|
1.0
|
N
|
A:HIS295
|
4.2
|
0.5
|
1.0
|
CA
|
A:CYS306
|
4.3
|
1.4
|
1.0
|
HA
|
A:ILE307
|
4.3
|
1.3
|
1.0
|
H
|
A:CYS310
|
4.3
|
0.8
|
1.0
|
HA
|
A:CYS306
|
4.3
|
1.6
|
1.0
|
HB2
|
A:CYS301
|
4.3
|
1.8
|
1.0
|
NE2
|
A:HIS295
|
4.4
|
0.7
|
1.0
|
H
|
A:LEU302
|
4.4
|
2.9
|
1.0
|
HB3
|
A:HIS295
|
4.4
|
0.5
|
1.0
|
CD2
|
A:HIS295
|
4.5
|
0.5
|
1.0
|
HB2
|
A:CYS306
|
4.6
|
2.3
|
1.0
|
O
|
A:THR293
|
4.6
|
1.2
|
1.0
|
CA
|
A:HIS295
|
4.6
|
0.5
|
1.0
|
N
|
A:ILE307
|
4.6
|
1.4
|
1.0
|
HA
|
A:TYR294
|
4.7
|
0.6
|
1.0
|
HG23
|
A:THR293
|
4.8
|
1.7
|
1.0
|
HB3
|
A:HIS309
|
4.8
|
0.7
|
1.0
|
N
|
A:CYS301
|
4.8
|
1.6
|
1.0
|
N
|
A:CYS310
|
4.8
|
0.8
|
1.0
|
CA
|
A:CYS310
|
4.8
|
0.6
|
1.0
|
HA
|
A:CYS298
|
4.9
|
0.9
|
1.0
|
ND1
|
A:HIS309
|
4.9
|
0.5
|
1.0
|
CA
|
A:ILE307
|
5.0
|
1.1
|
1.0
|
|
Zinc binding site 2 out
of 2 in 9dj8
Go back to
Zinc Binding Sites List in 9dj8
Zinc binding site 2 out
of 2 in the Rna-NSP9 Bound to the Niran Domain of the E-Rtc with An Empty G-Pocket
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Rna-NSP9 Bound to the Niran Domain of the E-Rtc with An Empty G-Pocket within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1002
b:23.4
occ:1.00
|
ND1
|
A:HIS642
|
2.1
|
3.9
|
1.0
|
SG
|
A:CYS645
|
2.2
|
7.1
|
1.0
|
SG
|
A:CYS646
|
2.4
|
6.8
|
1.0
|
SG
|
A:CYS487
|
2.4
|
8.4
|
1.0
|
CE1
|
A:HIS642
|
3.0
|
3.8
|
1.0
|
HB3
|
A:HIS642
|
3.1
|
4.0
|
1.0
|
HE1
|
A:HIS642
|
3.1
|
3.7
|
1.0
|
CG
|
A:HIS642
|
3.2
|
3.4
|
1.0
|
HB2
|
A:CYS645
|
3.4
|
7.1
|
1.0
|
HE1
|
A:PHE571
|
3.5
|
2.9
|
1.0
|
CB
|
A:CYS645
|
3.5
|
6.7
|
1.0
|
HB2
|
A:CYS646
|
3.5
|
5.9
|
1.0
|
H
|
A:CYS487
|
3.6
|
6.7
|
1.0
|
CB
|
A:CYS646
|
3.6
|
5.7
|
1.0
|
CB
|
A:HIS642
|
3.6
|
4.1
|
1.0
|
CB
|
A:CYS487
|
3.7
|
5.8
|
1.0
|
HB2
|
A:CYS487
|
3.7
|
6.3
|
1.0
|
HZ3
|
A:LYS532
|
3.9
|
3.8
|
1.0
|
C
|
A:CYS645
|
4.0
|
7.3
|
1.0
|
N
|
A:CYS487
|
4.0
|
6.6
|
1.0
|
N
|
A:CYS646
|
4.0
|
6.9
|
1.0
|
HA
|
A:HIS642
|
4.0
|
4.5
|
1.0
|
CE1
|
A:PHE571
|
4.1
|
2.8
|
1.0
|
NE2
|
A:HIS642
|
4.1
|
3.4
|
1.0
|
HA2
|
A:GLY486
|
4.2
|
4.1
|
1.0
|
HB3
|
A:CYS645
|
4.2
|
7.2
|
1.0
|
O
|
A:CYS645
|
4.2
|
8.7
|
1.0
|
CD2
|
A:HIS642
|
4.3
|
3.1
|
1.0
|
H
|
A:CYS646
|
4.3
|
7.0
|
1.0
|
CA
|
A:CYS645
|
4.3
|
6.1
|
1.0
|
CA
|
A:CYS646
|
4.3
|
5.2
|
1.0
|
HB3
|
A:CYS646
|
4.4
|
6.1
|
1.0
|
HB2
|
A:HIS642
|
4.4
|
4.0
|
1.0
|
HD1
|
A:PHE571
|
4.4
|
3.3
|
1.0
|
CA
|
A:CYS487
|
4.4
|
5.4
|
1.0
|
HZ1
|
A:LYS532
|
4.4
|
3.8
|
1.0
|
CA
|
A:HIS642
|
4.4
|
4.5
|
1.0
|
HB3
|
A:CYS487
|
4.5
|
6.3
|
1.0
|
CD1
|
A:PHE571
|
4.6
|
3.3
|
1.0
|
HA
|
A:CYS646
|
4.6
|
5.8
|
1.0
|
NZ
|
A:LYS532
|
4.6
|
3.9
|
1.0
|
HA
|
A:CYS487
|
4.6
|
5.9
|
1.0
|
H
|
A:CYS645
|
4.6
|
8.2
|
1.0
|
C
|
A:GLY486
|
4.8
|
4.5
|
1.0
|
CZ
|
A:PHE571
|
4.9
|
2.8
|
1.0
|
O
|
A:HIS642
|
4.9
|
7.3
|
1.0
|
CA
|
A:GLY486
|
4.9
|
3.8
|
1.0
|
HZ
|
A:PHE571
|
4.9
|
2.8
|
1.0
|
HE2
|
A:HIS642
|
4.9
|
3.4
|
1.0
|
N
|
A:CYS645
|
5.0
|
7.7
|
1.0
|
|
Reference:
G.I.Small,
S.A.Darst,
E.A.Campbell.
Matters Arising: There Is No Structure of the Catalytic Intermediate of Gtp-Mediated Mrna Capping By the Sars-Cov-2 Niran Domain, and Thus the Mechanism Remains Unknown To Be Published.
Page generated: Fri Aug 22 17:07:55 2025
|