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Potassium in PDB 4o6h: 2.8A Crystal Structure of Lymphocytic Choriomeningitis Virus Nucleoprotein C-Terminal Domain

Protein crystallography data

The structure of 2.8A Crystal Structure of Lymphocytic Choriomeningitis Virus Nucleoprotein C-Terminal Domain, PDB code: 4o6h 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) 47.26 / 2.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 92.856, 94.403, 145.124, 90.00, 102.30, 90.00
R / Rfree (%) 22.7 / 26.1

Other elements in 4o6h:

The structure of 2.8A Crystal Structure of Lymphocytic Choriomeningitis Virus Nucleoprotein C-Terminal Domain also contains other interesting chemical elements:

Magnesium (Mg) 4 atoms
Zinc (Zn) 8 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the 2.8A Crystal Structure of Lymphocytic Choriomeningitis Virus Nucleoprotein C-Terminal Domain (pdb code 4o6h). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the 2.8A Crystal Structure of Lymphocytic Choriomeningitis Virus Nucleoprotein C-Terminal Domain, PDB code: 4o6h:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in 4o6h

Go back to Potassium Binding Sites List in 4o6h
Potassium binding site 1 out of 4 in the 2.8A Crystal Structure of Lymphocytic Choriomeningitis Virus Nucleoprotein C-Terminal Domain


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of 2.8A Crystal Structure of Lymphocytic Choriomeningitis Virus Nucleoprotein C-Terminal Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K603

b:63.3
occ:1.00
HD22 C:ASN542 2.7 66.6 1.0
O C:LEU498 3.4 74.8 1.0
ND2 C:ASN542 3.5 55.5 1.0
ND1 C:HIS405 3.8 51.1 1.0
HE2 C:PHE403 3.8 57.7 1.0
HB2 C:ASN542 3.8 56.1 1.0
HD21 C:ASN542 3.9 66.6 1.0
HB3 C:HIS405 4.2 59.4 1.0
HZ C:PHE403 4.2 50.4 1.0
CB C:ASN542 4.4 46.7 1.0
HB3 C:ASN542 4.4 56.1 1.0
CG C:ASN542 4.4 45.5 1.0
HE1 C:HIS405 4.5 64.8 1.0
C C:LEU498 4.5 58.3 1.0
CE1 C:HIS405 4.5 54.0 1.0
CE2 C:PHE403 4.5 48.1 1.0
HA C:LEU498 4.6 69.9 1.0
HH C:TYR407 4.6 71.9 1.0
HD22 C:LEU520 4.6 57.4 1.0
HD22 C:LEU498 4.8 66.6 1.0
CG C:HIS405 4.8 48.2 1.0
CZ C:PHE403 4.8 42.0 1.0
CB C:HIS405 4.9 49.5 1.0
HB3 C:LEU498 4.9 57.0 1.0

Potassium binding site 2 out of 4 in 4o6h

Go back to Potassium Binding Sites List in 4o6h
Potassium binding site 2 out of 4 in the 2.8A Crystal Structure of Lymphocytic Choriomeningitis Virus Nucleoprotein C-Terminal Domain


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of 2.8A Crystal Structure of Lymphocytic Choriomeningitis Virus Nucleoprotein C-Terminal Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
D:K603

b:71.4
occ:1.00
HD22 D:ASN542 2.9 56.4 1.0
O D:LEU498 3.4 60.7 1.0
ND2 D:ASN542 3.6 47.0 1.0
HB2 D:ASN542 3.7 57.5 1.0
HE2 D:PHE403 3.7 58.1 1.0
HZ D:PHE403 3.9 50.6 1.0
ND1 D:HIS405 3.9 49.0 1.0
HB3 D:HIS405 4.0 56.8 1.0
HD21 D:ASN542 4.0 56.4 1.0
HB3 D:ASN542 4.2 57.5 1.0
CB D:ASN542 4.3 47.9 1.0
CG D:ASN542 4.4 47.0 1.0
CE2 D:PHE403 4.4 48.5 1.0
HA D:LEU498 4.5 67.9 1.0
CZ D:PHE403 4.5 42.2 1.0
C D:LEU498 4.5 53.5 1.0
HD22 D:LEU520 4.6 59.5 1.0
HD22 D:LEU498 4.6 60.7 1.0
HH D:TYR407 4.6 74.0 1.0
HD23 D:LEU498 4.8 60.7 1.0
CB D:HIS405 4.8 47.4 1.0
HB3 D:LEU498 4.8 65.6 1.0
CG D:HIS405 4.8 45.1 1.0
CE1 D:HIS405 4.8 53.9 1.0
HE1 D:HIS405 4.9 64.7 1.0
HD21 D:LEU520 4.9 59.5 1.0
HD23 D:LEU520 5.0 59.5 1.0

Potassium binding site 3 out of 4 in 4o6h

Go back to Potassium Binding Sites List in 4o6h
Potassium binding site 3 out of 4 in the 2.8A Crystal Structure of Lymphocytic Choriomeningitis Virus Nucleoprotein C-Terminal Domain


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of 2.8A Crystal Structure of Lymphocytic Choriomeningitis Virus Nucleoprotein C-Terminal Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
G:K603

b:85.7
occ:1.00
HD22 G:ASN542 2.7 71.2 1.0
ND2 G:ASN542 3.5 59.3 1.0
O G:LEU498 3.8 79.7 1.0
HZ G:PHE403 3.8 75.8 1.0
HB2 G:ASN542 3.9 75.6 1.0
HD21 G:ASN542 3.9 71.2 1.0
HB3 G:HIS405 4.0 72.0 1.0
ND1 G:HIS405 4.0 62.6 1.0
HE2 G:PHE403 4.1 75.6 1.0
HH G:TYR407 4.4 91.0 1.0
HB3 G:ASN542 4.5 75.6 1.0
CB G:ASN542 4.5 63.0 1.0
CZ G:PHE403 4.5 63.2 1.0
CG G:ASN542 4.5 59.6 1.0
CE2 G:PHE403 4.7 63.0 1.0
HD22 G:LEU498 4.7 82.9 1.0
OH G:TYR407 4.7 75.9 1.0
HA G:LEU498 4.8 90.9 1.0
C G:LEU498 4.8 72.8 1.0
CB G:HIS405 4.8 60.0 1.0
HD22 G:LEU520 4.9 73.4 1.0
CG G:HIS405 4.9 60.9 1.0
CE1 G:HIS405 4.9 69.1 1.0
HE1 G:HIS405 5.0 82.9 1.0
HD23 G:LEU498 5.0 82.9 1.0
HB3 G:LEU498 5.0 84.7 1.0

Potassium binding site 4 out of 4 in 4o6h

Go back to Potassium Binding Sites List in 4o6h
Potassium binding site 4 out of 4 in the 2.8A Crystal Structure of Lymphocytic Choriomeningitis Virus Nucleoprotein C-Terminal Domain


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of 2.8A Crystal Structure of Lymphocytic Choriomeningitis Virus Nucleoprotein C-Terminal Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
H:K603

b:89.9
occ:1.00
HD22 H:ASN542 3.1 74.0 1.0
HZ H:PHE403 3.7 82.3 1.0
O H:LEU498 3.7 86.3 1.0
ND2 H:ASN542 3.9 61.7 1.0
ND1 H:HIS405 4.1 76.0 1.0
HE2 H:PHE403 4.1 84.4 1.0
HB2 H:ASN542 4.1 83.5 1.0
HB3 H:HIS405 4.2 83.1 1.0
HD21 H:ASN542 4.3 74.0 1.0
CZ H:PHE403 4.5 68.6 1.0
HH H:TYR407 4.5 97.2 1.0
HA H:LEU498 4.6 95.8 1.0
HD22 H:LEU498 4.6 86.9 1.0
CE2 H:PHE403 4.6 70.3 1.0
C H:LEU498 4.7 81.9 1.0
CB H:ASN542 4.7 69.6 1.0
HB3 H:ASN542 4.8 83.5 1.0
CG H:ASN542 4.8 68.3 1.0
HE1 H:HIS405 4.9 93.0 1.0
HD22 H:LEU520 4.9 84.8 1.0
OH H:TYR407 4.9 81.0 1.0
HD23 H:LEU498 4.9 86.9 1.0
CE1 H:HIS405 4.9 77.5 1.0
CG H:HIS405 5.0 70.4 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: Mon Aug 12 11:41:51 2024

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