Zinc in PDB 4o6i: 2.0A Crystal Structure of Lymphocytic Choriomeningitis Virus Nucleoprotein C-Terminal Domain
Protein crystallography data
The structure of 2.0A Crystal Structure of Lymphocytic Choriomeningitis Virus Nucleoprotein C-Terminal Domain, PDB code: 4o6i
was solved by
B.R.West,
K.M.Hastie,
E.O.Saphire,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
38.95 /
2.00
|
Space group
|
P 65
|
Cell size a, b, c (Å), α, β, γ (°)
|
89.962,
89.962,
145.941,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
20.9 /
22.8
|
Other elements in 4o6i:
The structure of 2.0A Crystal Structure of Lymphocytic Choriomeningitis Virus Nucleoprotein C-Terminal Domain also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the 2.0A Crystal Structure of Lymphocytic Choriomeningitis Virus Nucleoprotein C-Terminal Domain
(pdb code 4o6i). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the
2.0A Crystal Structure of Lymphocytic Choriomeningitis Virus Nucleoprotein C-Terminal Domain, PDB code: 4o6i:
Jump to Zinc binding site number:
1;
2;
Zinc binding site 1 out
of 2 in 4o6i
Go back to
Zinc Binding Sites List in 4o6i
Zinc binding site 1 out
of 2 in the 2.0A Crystal Structure of Lymphocytic Choriomeningitis Virus Nucleoprotein C-Terminal Domain
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of 2.0A Crystal Structure of Lymphocytic Choriomeningitis Virus Nucleoprotein C-Terminal Domain within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn601
b:54.0
occ:1.00
|
OE2
|
A:GLU392
|
2.0
|
51.7
|
1.0
|
NE2
|
A:HIS502
|
2.0
|
61.6
|
1.0
|
SG
|
A:CYS518
|
2.2
|
49.7
|
1.0
|
SG
|
A:CYS499
|
2.3
|
48.1
|
1.0
|
CD
|
A:GLU392
|
2.9
|
48.9
|
1.0
|
CD2
|
A:HIS502
|
3.0
|
55.7
|
1.0
|
HB2
|
A:CYS518
|
3.1
|
66.6
|
1.0
|
CE1
|
A:HIS502
|
3.1
|
55.2
|
1.0
|
HD2
|
A:HIS502
|
3.1
|
66.9
|
1.0
|
OE1
|
A:GLU392
|
3.1
|
51.7
|
1.0
|
CB
|
A:CYS518
|
3.2
|
55.5
|
1.0
|
HB3
|
A:CYS499
|
3.2
|
65.6
|
1.0
|
CB
|
A:CYS499
|
3.3
|
54.7
|
1.0
|
HE1
|
A:HIS502
|
3.3
|
66.2
|
1.0
|
HE2
|
A:HIS405
|
3.4
|
68.6
|
1.0
|
HA
|
A:CYS518
|
3.4
|
65.4
|
1.0
|
HB2
|
A:CYS499
|
3.5
|
65.6
|
1.0
|
HE1
|
A:TYR407
|
3.6
|
66.9
|
1.0
|
HE1
|
A:HIS405
|
3.7
|
67.5
|
1.0
|
H
|
A:ALA519
|
3.8
|
65.0
|
1.0
|
CA
|
A:CYS518
|
3.8
|
54.5
|
1.0
|
HH
|
A:TYR407
|
4.0
|
67.5
|
1.0
|
NE2
|
A:HIS405
|
4.0
|
57.2
|
1.0
|
HB3
|
A:CYS518
|
4.0
|
66.6
|
1.0
|
H
|
A:LEU520
|
4.0
|
56.6
|
1.0
|
HB2
|
A:MET501
|
4.1
|
71.3
|
1.0
|
CG
|
A:HIS502
|
4.1
|
61.9
|
1.0
|
ND1
|
A:HIS502
|
4.1
|
61.6
|
1.0
|
CE1
|
A:HIS405
|
4.2
|
56.3
|
1.0
|
N
|
A:ALA519
|
4.3
|
54.2
|
1.0
|
CG
|
A:GLU392
|
4.3
|
56.6
|
1.0
|
HB3
|
A:LEU520
|
4.4
|
59.7
|
1.0
|
C
|
A:CYS518
|
4.4
|
52.8
|
1.0
|
HG3
|
A:GLU392
|
4.5
|
67.9
|
1.0
|
CE1
|
A:TYR407
|
4.5
|
55.7
|
1.0
|
H
|
A:MET501
|
4.7
|
71.7
|
1.0
|
HG2
|
A:GLU392
|
4.7
|
67.9
|
1.0
|
CA
|
A:CYS499
|
4.7
|
52.0
|
1.0
|
HH2
|
A:TRP492
|
4.8
|
64.6
|
1.0
|
OH
|
A:TYR407
|
4.8
|
56.3
|
1.0
|
HG2
|
A:MET521
|
4.8
|
54.1
|
1.0
|
N
|
A:LEU520
|
4.9
|
47.2
|
1.0
|
H
|
A:MET521
|
4.9
|
61.3
|
1.0
|
HD1
|
A:HIS502
|
4.9
|
73.9
|
1.0
|
|
Zinc binding site 2 out
of 2 in 4o6i
Go back to
Zinc Binding Sites List in 4o6i
Zinc binding site 2 out
of 2 in the 2.0A Crystal Structure of Lymphocytic Choriomeningitis Virus Nucleoprotein C-Terminal Domain
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of 2.0A Crystal Structure of Lymphocytic Choriomeningitis Virus Nucleoprotein C-Terminal Domain within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn601
b:54.0
occ:1.00
|
OE2
|
B:GLU392
|
2.0
|
51.9
|
1.0
|
NE2
|
B:HIS502
|
2.0
|
60.6
|
1.0
|
SG
|
B:CYS518
|
2.2
|
52.4
|
1.0
|
SG
|
B:CYS499
|
2.3
|
55.0
|
1.0
|
CD
|
B:GLU392
|
2.9
|
51.1
|
1.0
|
CD2
|
B:HIS502
|
3.0
|
57.7
|
1.0
|
HB2
|
B:CYS518
|
3.0
|
70.9
|
1.0
|
CE1
|
B:HIS502
|
3.1
|
57.3
|
1.0
|
OE1
|
B:GLU392
|
3.1
|
54.2
|
1.0
|
HD2
|
B:HIS502
|
3.1
|
69.2
|
1.0
|
CB
|
B:CYS518
|
3.2
|
59.1
|
1.0
|
HB3
|
B:CYS499
|
3.2
|
64.3
|
1.0
|
HE1
|
B:HIS502
|
3.3
|
68.7
|
1.0
|
CB
|
B:CYS499
|
3.3
|
53.6
|
1.0
|
HE2
|
B:HIS405
|
3.3
|
69.1
|
1.0
|
HA
|
B:CYS518
|
3.4
|
69.8
|
1.0
|
HB2
|
B:CYS499
|
3.5
|
64.3
|
1.0
|
HE1
|
B:TYR407
|
3.5
|
64.5
|
1.0
|
HE1
|
B:HIS405
|
3.7
|
70.0
|
1.0
|
CA
|
B:CYS518
|
3.8
|
58.1
|
1.0
|
H
|
B:ALA519
|
3.9
|
67.8
|
1.0
|
HB2
|
B:MET501
|
3.9
|
71.7
|
1.0
|
NE2
|
B:HIS405
|
4.0
|
57.6
|
1.0
|
HB3
|
B:CYS518
|
4.0
|
70.9
|
1.0
|
HH
|
B:TYR407
|
4.0
|
66.4
|
1.0
|
CG
|
B:HIS502
|
4.1
|
61.7
|
1.0
|
ND1
|
B:HIS502
|
4.1
|
61.0
|
1.0
|
H
|
B:LEU520
|
4.2
|
65.2
|
1.0
|
CE1
|
B:HIS405
|
4.2
|
58.3
|
1.0
|
CG
|
B:GLU392
|
4.3
|
54.3
|
1.0
|
N
|
B:ALA519
|
4.4
|
56.5
|
1.0
|
CE1
|
B:TYR407
|
4.5
|
53.8
|
1.0
|
HG3
|
B:GLU392
|
4.5
|
65.1
|
1.0
|
C
|
B:CYS518
|
4.5
|
53.7
|
1.0
|
HB3
|
B:LEU520
|
4.5
|
59.6
|
1.0
|
H
|
B:MET501
|
4.6
|
64.2
|
1.0
|
HG2
|
B:GLU392
|
4.7
|
65.1
|
1.0
|
CA
|
B:CYS499
|
4.7
|
51.5
|
1.0
|
HH2
|
B:TRP492
|
4.8
|
68.2
|
1.0
|
HE2
|
B:MET426
|
4.8
|
71.5
|
1.0
|
OH
|
B:TYR407
|
4.8
|
55.3
|
1.0
|
HG2
|
B:MET521
|
4.8
|
57.8
|
1.0
|
CB
|
B:MET501
|
4.9
|
59.8
|
1.0
|
HD1
|
B:HIS502
|
4.9
|
73.2
|
1.0
|
HG3
|
B:MET501
|
5.0
|
72.0
|
1.0
|
HA
|
B:CYS499
|
5.0
|
61.8
|
1.0
|
|
Reference:
B.R.West,
K.M.Hastie,
E.O.Saphire.
Structure of the Lcmv Nucleoprotein Provides A Template For Understanding Arenavirus Replication and Immunosuppression. Acta Crystallogr.,Sect.D V. 70 1764 2014.
ISSN: ISSN 0907-4449
PubMed: 24914986
DOI: 10.1107/S1399004714007883
Page generated: Sun Oct 27 03:33:05 2024
|