Zinc in PDB 8sqj: Sars-Cov-2 Replication-Transcription Complex Bound to Rna-NSP9, As A Noncatalytic Rna-NSP9 Binding Mode
Enzymatic activity of Sars-Cov-2 Replication-Transcription Complex Bound to Rna-NSP9, As A Noncatalytic Rna-NSP9 Binding Mode
All present enzymatic activity of Sars-Cov-2 Replication-Transcription Complex Bound to Rna-NSP9, As A Noncatalytic Rna-NSP9 Binding Mode:
2.7.7.48;
Other elements in 8sqj:
The structure of Sars-Cov-2 Replication-Transcription Complex Bound to Rna-NSP9, As A Noncatalytic Rna-NSP9 Binding Mode also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Sars-Cov-2 Replication-Transcription Complex Bound to Rna-NSP9, As A Noncatalytic Rna-NSP9 Binding Mode
(pdb code 8sqj). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the
Sars-Cov-2 Replication-Transcription Complex Bound to Rna-NSP9, As A Noncatalytic Rna-NSP9 Binding Mode, PDB code: 8sqj:
Jump to Zinc binding site number:
1;
2;
Zinc binding site 1 out
of 2 in 8sqj
Go back to
Zinc Binding Sites List in 8sqj
Zinc binding site 1 out
of 2 in the Sars-Cov-2 Replication-Transcription Complex Bound to Rna-NSP9, As A Noncatalytic Rna-NSP9 Binding Mode
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Sars-Cov-2 Replication-Transcription Complex Bound to Rna-NSP9, As A Noncatalytic Rna-NSP9 Binding Mode within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1003
b:93.0
occ:1.00
|
O
|
A:HOH1159
|
1.8
|
37.4
|
1.0
|
ND1
|
A:HIS295
|
2.3
|
29.2
|
1.0
|
SG
|
A:CYS301
|
2.3
|
31.1
|
1.0
|
SG
|
A:CYS310
|
2.3
|
30.2
|
1.0
|
SG
|
A:CYS306
|
2.3
|
41.2
|
1.0
|
O
|
A:CYS306
|
3.0
|
39.4
|
1.0
|
HB2
|
A:HIS295
|
3.1
|
19.6
|
1.0
|
CE1
|
A:HIS295
|
3.2
|
13.2
|
1.0
|
HE1
|
A:HIS295
|
3.3
|
19.0
|
1.0
|
HA
|
A:CYS301
|
3.3
|
26.2
|
1.0
|
CG
|
A:HIS295
|
3.3
|
20.6
|
1.0
|
CB
|
A:CYS301
|
3.5
|
24.9
|
1.0
|
HB3
|
A:CYS301
|
3.5
|
27.5
|
1.0
|
H
|
A:HIS295
|
3.6
|
21.0
|
1.0
|
CB
|
A:HIS295
|
3.7
|
16.9
|
1.0
|
CB
|
A:CYS310
|
3.8
|
23.3
|
1.0
|
HB2
|
A:CYS310
|
3.8
|
25.4
|
1.0
|
CB
|
A:CYS306
|
3.9
|
20.5
|
1.0
|
CA
|
A:CYS301
|
3.9
|
17.8
|
1.0
|
C
|
A:CYS306
|
3.9
|
27.8
|
1.0
|
HB3
|
A:CYS306
|
4.1
|
29.4
|
1.0
|
HB3
|
A:CYS310
|
4.2
|
23.7
|
1.0
|
N
|
A:HIS295
|
4.2
|
22.1
|
1.0
|
HD1
|
A:HIS309
|
4.3
|
24.3
|
1.0
|
HB2
|
A:CYS301
|
4.3
|
26.4
|
1.0
|
NE2
|
A:HIS295
|
4.3
|
17.6
|
1.0
|
H
|
A:CYS310
|
4.4
|
24.3
|
1.0
|
H
|
A:LEU302
|
4.4
|
31.0
|
1.0
|
CA
|
A:CYS306
|
4.4
|
22.4
|
1.0
|
HB3
|
A:HIS295
|
4.4
|
20.6
|
1.0
|
CD2
|
A:HIS295
|
4.4
|
21.7
|
1.0
|
HA
|
A:CYS306
|
4.5
|
29.8
|
1.0
|
HA
|
A:ILE307
|
4.6
|
25.6
|
1.0
|
HB2
|
A:CYS306
|
4.6
|
29.7
|
1.0
|
CA
|
A:HIS295
|
4.6
|
12.3
|
1.0
|
HG23
|
A:THR293
|
4.7
|
27.3
|
1.0
|
HA
|
A:TYR294
|
4.7
|
18.9
|
1.0
|
O
|
A:THR293
|
4.7
|
31.8
|
1.0
|
N
|
A:CYS301
|
4.7
|
28.4
|
1.0
|
HG
|
A:LEU302
|
4.8
|
30.4
|
1.0
|
HA
|
A:CYS298
|
4.9
|
23.4
|
1.0
|
HB3
|
A:HIS309
|
4.9
|
24.5
|
1.0
|
N
|
A:CYS310
|
4.9
|
19.9
|
1.0
|
N
|
A:ILE307
|
4.9
|
29.8
|
1.0
|
CA
|
A:CYS310
|
5.0
|
12.1
|
1.0
|
N
|
A:LEU302
|
5.0
|
32.9
|
1.0
|
H
|
A:CYS301
|
5.0
|
27.0
|
1.0
|
|
Zinc binding site 2 out
of 2 in 8sqj
Go back to
Zinc Binding Sites List in 8sqj
Zinc binding site 2 out
of 2 in the Sars-Cov-2 Replication-Transcription Complex Bound to Rna-NSP9, As A Noncatalytic Rna-NSP9 Binding Mode
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Sars-Cov-2 Replication-Transcription Complex Bound to Rna-NSP9, As A Noncatalytic Rna-NSP9 Binding Mode within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1004
b:80.7
occ:1.00
|
ND1
|
A:HIS642
|
2.2
|
30.2
|
1.0
|
SG
|
A:CYS487
|
2.3
|
44.2
|
1.0
|
SG
|
A:CYS645
|
2.3
|
38.3
|
1.0
|
SG
|
A:CYS646
|
2.3
|
49.0
|
1.0
|
HB3
|
A:HIS642
|
2.7
|
29.9
|
1.0
|
CG
|
A:HIS642
|
3.1
|
23.8
|
1.0
|
CE1
|
A:HIS642
|
3.2
|
29.2
|
1.0
|
HE1
|
A:HIS642
|
3.4
|
30.6
|
1.0
|
CB
|
A:HIS642
|
3.4
|
24.7
|
1.0
|
HE1
|
A:PHE571
|
3.5
|
25.7
|
1.0
|
CB
|
A:CYS487
|
3.8
|
38.4
|
1.0
|
H
|
A:CYS487
|
3.8
|
36.2
|
1.0
|
CB
|
A:CYS646
|
3.8
|
32.9
|
1.0
|
CB
|
A:CYS645
|
3.8
|
41.0
|
1.0
|
HB2
|
A:CYS646
|
3.9
|
37.1
|
1.0
|
HB2
|
A:CYS487
|
3.9
|
37.7
|
1.0
|
HB2
|
A:CYS645
|
3.9
|
41.1
|
1.0
|
N
|
A:CYS487
|
4.1
|
31.6
|
1.0
|
CE1
|
A:PHE571
|
4.1
|
24.0
|
1.0
|
HA
|
A:HIS642
|
4.1
|
31.4
|
1.0
|
HB2
|
A:HIS642
|
4.1
|
29.7
|
1.0
|
HA2
|
A:GLY486
|
4.2
|
31.7
|
1.0
|
HZ3
|
A:LYS532
|
4.2
|
30.9
|
1.0
|
HD1
|
A:PHE571
|
4.3
|
26.3
|
1.0
|
NE2
|
A:HIS642
|
4.3
|
23.7
|
1.0
|
CD2
|
A:HIS642
|
4.3
|
22.0
|
1.0
|
N
|
A:CYS646
|
4.3
|
38.8
|
1.0
|
C
|
A:CYS645
|
4.3
|
41.7
|
1.0
|
CA
|
A:HIS642
|
4.4
|
32.0
|
1.0
|
CA
|
A:CYS487
|
4.4
|
36.3
|
1.0
|
HB3
|
A:CYS487
|
4.5
|
37.0
|
1.0
|
H
|
A:CYS646
|
4.5
|
38.3
|
1.0
|
CD1
|
A:PHE571
|
4.5
|
23.8
|
1.0
|
HB3
|
A:CYS646
|
4.5
|
36.9
|
1.0
|
HB3
|
A:CYS645
|
4.5
|
41.3
|
1.0
|
HE2
|
A:LYS532
|
4.5
|
29.5
|
1.0
|
HA
|
A:CYS487
|
4.6
|
36.5
|
1.0
|
C
|
A:GLY486
|
4.6
|
30.5
|
1.0
|
CA
|
A:CYS646
|
4.6
|
31.4
|
1.0
|
CA
|
A:CYS645
|
4.7
|
41.4
|
1.0
|
O
|
A:CYS645
|
4.7
|
45.1
|
1.0
|
H
|
A:CYS645
|
4.7
|
42.0
|
1.0
|
CA
|
A:GLY486
|
4.9
|
25.7
|
1.0
|
NZ
|
A:LYS532
|
4.9
|
40.1
|
1.0
|
HZ2
|
A:LYS532
|
4.9
|
30.8
|
1.0
|
CZ
|
A:PHE571
|
4.9
|
18.3
|
1.0
|
O
|
A:HIS642
|
4.9
|
38.2
|
1.0
|
HA
|
A:CYS646
|
4.9
|
37.2
|
1.0
|
HZ
|
A:PHE528
|
5.0
|
28.3
|
1.0
|
|
Reference:
G.I.Small,
O.Fedorova,
P.D.B.Olinares,
J.Chandanani,
A.Banerjee,
Y.J.Choi,
H.Molina,
B.T.Chait,
S.A.Darst,
E.A.Campbell.
Structural and Functional Insights Into the Enzymatic Plasticity of the Sars-Cov-2 Niran Domain. Mol.Cell V. 83 3921 2023.
ISSN: ISSN 1097-2765
PubMed: 37890482
DOI: 10.1016/J.MOLCEL.2023.10.001
Page generated: Thu Oct 31 11:07:55 2024
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