Zinc in PDB 8xj6: The Cryo-Em Structure of Mpxv E5 Apo Conformation
Zinc Binding Sites:
The binding sites of Zinc atom in the The Cryo-Em Structure of Mpxv E5 Apo Conformation
(pdb code 8xj6). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the
The Cryo-Em Structure of Mpxv E5 Apo Conformation, PDB code: 8xj6:
Jump to Zinc binding site number:
1;
2;
Zinc binding site 1 out
of 2 in 8xj6
Go back to
Zinc Binding Sites List in 8xj6
Zinc binding site 1 out
of 2 in the The Cryo-Em Structure of Mpxv E5 Apo Conformation
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of The Cryo-Em Structure of Mpxv E5 Apo Conformation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Zn802
b:30.0
occ:1.00
|
SG
|
E:CYS285
|
2.5
|
145.0
|
1.0
|
ND1
|
E:HIS290
|
2.5
|
143.6
|
1.0
|
SG
|
E:CYS314
|
2.7
|
136.2
|
1.0
|
CB
|
E:CYS285
|
2.8
|
145.0
|
1.0
|
CE1
|
E:HIS290
|
2.8
|
143.6
|
1.0
|
SG
|
E:CYS282
|
2.9
|
151.9
|
1.0
|
CE1
|
E:HIS294
|
3.5
|
134.7
|
1.0
|
N
|
E:CYS285
|
3.6
|
145.0
|
1.0
|
NE2
|
E:HIS294
|
3.6
|
134.7
|
1.0
|
CB
|
E:CYS314
|
3.6
|
136.2
|
1.0
|
CA
|
E:CYS285
|
3.8
|
145.0
|
1.0
|
CB
|
E:CYS282
|
3.8
|
151.9
|
1.0
|
CG
|
E:HIS290
|
3.8
|
143.6
|
1.0
|
NE2
|
E:HIS290
|
4.1
|
143.6
|
1.0
|
CA
|
E:CYS314
|
4.5
|
136.2
|
1.0
|
CB
|
E:LEU284
|
4.5
|
141.9
|
1.0
|
CB
|
E:HIS290
|
4.5
|
143.6
|
1.0
|
C
|
E:LEU284
|
4.6
|
141.9
|
1.0
|
CD2
|
E:HIS290
|
4.6
|
143.6
|
1.0
|
ND1
|
E:HIS294
|
4.8
|
134.7
|
1.0
|
C
|
E:CYS285
|
4.8
|
145.0
|
1.0
|
O
|
E:SER313
|
4.9
|
134.6
|
1.0
|
CA
|
E:LEU284
|
5.0
|
141.9
|
1.0
|
CD2
|
E:HIS294
|
5.0
|
134.7
|
1.0
|
|
Zinc binding site 2 out
of 2 in 8xj6
Go back to
Zinc Binding Sites List in 8xj6
Zinc binding site 2 out
of 2 in the The Cryo-Em Structure of Mpxv E5 Apo Conformation
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of The Cryo-Em Structure of Mpxv E5 Apo Conformation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Zn802
b:30.0
occ:1.00
|
SG
|
F:CYS285
|
2.2
|
151.9
|
1.0
|
SG
|
F:CYS314
|
2.4
|
142.7
|
1.0
|
SG
|
F:CYS282
|
2.4
|
154.6
|
1.0
|
CB
|
F:CYS285
|
3.0
|
151.9
|
1.0
|
CB
|
F:CYS282
|
3.0
|
154.6
|
1.0
|
CB
|
F:CYS314
|
3.2
|
142.7
|
1.0
|
CA
|
F:CYS314
|
4.0
|
142.7
|
1.0
|
N
|
F:CYS285
|
4.1
|
151.9
|
1.0
|
CA
|
F:CYS285
|
4.1
|
151.9
|
1.0
|
CA
|
F:CYS282
|
4.3
|
154.6
|
1.0
|
O
|
F:CYS282
|
4.4
|
154.6
|
1.0
|
CE1
|
F:HIS294
|
4.5
|
146.4
|
1.0
|
NE2
|
F:HIS294
|
4.5
|
146.4
|
1.0
|
CB
|
F:HIS290
|
4.6
|
151.7
|
1.0
|
CB
|
F:LYS287
|
4.6
|
153.6
|
1.0
|
C
|
F:CYS282
|
4.6
|
154.6
|
1.0
|
C
|
F:CYS285
|
4.8
|
151.9
|
1.0
|
N
|
F:CYS282
|
4.8
|
154.6
|
1.0
|
O
|
F:SER313
|
4.9
|
145.0
|
1.0
|
N
|
F:CYS314
|
4.9
|
142.7
|
1.0
|
N
|
F:LYS287
|
5.0
|
153.6
|
1.0
|
C
|
F:LEU284
|
5.0
|
148.1
|
1.0
|
|
Reference:
J.Gan,
W.Zhang.
Structural and Functional Insights Into the Helicase Protein E5 of Mpox Virus. Cell Discov 2024.
ISSN: ESSN 2056-5968
Page generated: Thu Oct 31 13:54:00 2024
|