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Potassium in PDB 1s72: Refined Crystal Structure of the Haloarcula Marismortui Large Ribosomal Subunit at 2.4 Angstrom Resolution

Protein crystallography data

The structure of Refined Crystal Structure of the Haloarcula Marismortui Large Ribosomal Subunit at 2.4 Angstrom Resolution, PDB code: 1s72 was solved by D.J.Klein, T.M.Schmeing, P.B.Moore, T.A.Steitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 2.40
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 211.660, 299.670, 573.770, 90.00, 90.00, 90.00
R / Rfree (%) 18.8 / 22.2

Other elements in 1s72:

The structure of Refined Crystal Structure of the Haloarcula Marismortui Large Ribosomal Subunit at 2.4 Angstrom Resolution also contains other interesting chemical elements:

Magnesium (Mg) 116 atoms
Cadmium (Cd) 5 atoms
Chlorine (Cl) 22 atoms
Sodium (Na) 86 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Refined Crystal Structure of the Haloarcula Marismortui Large Ribosomal Subunit at 2.4 Angstrom Resolution (pdb code 1s72). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Refined Crystal Structure of the Haloarcula Marismortui Large Ribosomal Subunit at 2.4 Angstrom Resolution, PDB code: 1s72:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 1s72

Go back to Potassium Binding Sites List in 1s72
Potassium binding site 1 out of 2 in the Refined Crystal Structure of the Haloarcula Marismortui Large Ribosomal Subunit at 2.4 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Refined Crystal Structure of the Haloarcula Marismortui Large Ribosomal Subunit at 2.4 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
0:K8201

b:64.8
occ:1.00
O6 0:G2102 2.8 32.4 1.0
O6 0:G2482 2.9 25.7 1.0
N7 0:G2482 3.0 22.3 1.0
O2 0:C2536 3.2 24.6 1.0
O4' 0:C2536 3.3 28.1 1.0
N7 0:G2102 3.4 32.8 1.0
C6 0:G2102 3.5 33.4 1.0
C6 0:G2482 3.6 23.0 1.0
C5 0:G2482 3.6 23.4 1.0
C5 0:G2102 3.8 33.8 1.0
C2 0:C2536 3.8 26.7 1.0
C1' 0:C2536 3.8 27.7 1.0
N6 0:A2486 4.0 40.5 1.0
C4' 0:C2536 4.1 27.8 1.0
N1 0:C2536 4.1 28.7 1.0
O2 0:U2535 4.1 33.3 1.0
C8 0:G2482 4.2 23.4 1.0
C2 0:U2535 4.4 29.9 1.0
OP1 0:U2539 4.5 25.5 1.0
C8 0:G2102 4.6 35.3 1.0
C5' 0:C2536 4.6 27.2 1.0
N3 0:C2536 4.7 28.2 1.0
N3 0:U2535 4.7 27.5 1.0
C2' 0:U2535 4.7 30.6 1.0
N1 0:G2102 4.8 33.8 1.0
N1 0:G2482 4.9 21.8 1.0
C4 0:G2482 4.9 23.1 1.0

Potassium binding site 2 out of 2 in 1s72

Go back to Potassium Binding Sites List in 1s72
Potassium binding site 2 out of 2 in the Refined Crystal Structure of the Haloarcula Marismortui Large Ribosomal Subunit at 2.4 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Refined Crystal Structure of the Haloarcula Marismortui Large Ribosomal Subunit at 2.4 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
0:K8202

b:38.7
occ:1.00
O 0:HOH8535 2.8 12.0 1.0
O4 0:U163 2.9 21.3 1.0
O 0:HOH8631 2.9 22.8 1.0
O4 0:U172 3.0 24.7 1.0
O 0:HOH8665 3.0 16.7 1.0
O 0:HOH4450 3.1 38.9 1.0
OP2 0:C162 3.1 20.5 1.0
O 0:HOH7325 3.3 26.8 1.0
CD M:ARG82 3.7 23.1 1.0
C4 0:U172 3.9 25.9 1.0
C4 0:U163 3.9 21.4 1.0
O 0:HOH8843 3.9 25.5 1.0
N3 0:U172 4.0 24.5 1.0
O 0:HOH7324 4.0 21.0 1.0
N4 0:C171 4.3 22.8 1.0
NE M:ARG82 4.4 24.7 1.0
C5 0:U163 4.4 22.3 1.0
P 0:C162 4.4 20.6 1.0
O6 0:G164 4.4 23.0 1.0
OP2 0:A169 4.4 21.8 1.0
MG 0:MG8054 4.7 18.5 1.0
CB M:ARG82 4.8 22.8 1.0
CG M:ARG82 4.8 23.2 1.0
OP1 0:C162 4.8 23.9 1.0
N3 0:C173 4.9 19.1 1.0
N4 0:C173 4.9 19.0 1.0
OP1 0:A169 4.9 21.8 1.0

Reference:

D.J.Klein, P.B.Moore, T.A.Steitz. The Roles of Ribosomal Proteins in the Structure, Assembly and Evolution of the Large Ribosomal Subunit J.Mol.Biol. V. 340 141 2004.
ISSN: ISSN 0022-2836
PubMed: 15184028
DOI: 10.1016/J.JMB.2004.03.076
Page generated: Mon Aug 12 05:22:49 2024

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