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Potassium in PDB 1yj9: Crystal Structure of the Mutant 50S Ribosomal Subunit of Haloarcula Marismortui Containing A Three Residue Deletion in L22

Protein crystallography data

The structure of Crystal Structure of the Mutant 50S Ribosomal Subunit of Haloarcula Marismortui Containing A Three Residue Deletion in L22, PDB code: 1yj9 was solved by D.Tu, G.Blaha, 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) 29.94 / 2.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 213.076, 300.750, 575.478, 90.00, 90.00, 90.00
R / Rfree (%) 18.4 / 24.2

Other elements in 1yj9:

The structure of Crystal Structure of the Mutant 50S Ribosomal Subunit of Haloarcula Marismortui Containing A Three Residue Deletion in L22 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 Crystal Structure of the Mutant 50S Ribosomal Subunit of Haloarcula Marismortui Containing A Three Residue Deletion in L22 (pdb code 1yj9). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of the Mutant 50S Ribosomal Subunit of Haloarcula Marismortui Containing A Three Residue Deletion in L22, PDB code: 1yj9:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 1yj9

Go back to Potassium Binding Sites List in 1yj9
Potassium binding site 1 out of 2 in the Crystal Structure of the Mutant 50S Ribosomal Subunit of Haloarcula Marismortui Containing A Three Residue Deletion in L22


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of the Mutant 50S Ribosomal Subunit of Haloarcula Marismortui Containing A Three Residue Deletion in L22 within 5.0Å range:
probe atom residue distance (Å) B Occ
0:K8401

b:91.7
occ:1.00
O6 0:G2482 2.5 43.4 1.0
O6 0:G2102 2.5 51.8 1.0
N7 0:G2482 3.0 43.5 1.0
O2 0:C2536 3.2 35.3 1.0
C6 0:G2482 3.2 42.5 1.0
C6 0:G2102 3.4 51.1 1.0
C5 0:G2482 3.5 43.5 1.0
O4' 0:C2536 3.6 36.2 1.0
N7 0:G2102 3.7 49.9 1.0
C2 0:C2536 3.7 36.9 1.0
N6 0:A2486 3.8 55.4 1.0
C5 0:G2102 3.9 50.6 1.0
C1' 0:C2536 3.9 35.3 1.0
N1 0:C2536 4.1 36.9 1.0
O2 0:U2535 4.1 43.4 1.0
C8 0:G2482 4.3 43.2 1.0
C2 0:U2535 4.3 41.9 1.0
C4' 0:C2536 4.4 36.1 1.0
N3 0:U2535 4.5 40.2 1.0
OP1 0:U2539 4.5 47.0 1.0
N3 0:C2536 4.5 37.3 1.0
N1 0:G2482 4.6 42.3 1.0
N1 0:G2102 4.6 51.6 1.0
C2' 0:U2535 4.8 42.5 1.0
C4 0:G2482 4.8 44.1 1.0
N1 0:U2535 4.9 42.5 1.0
C8 0:G2102 4.9 50.1 1.0

Potassium binding site 2 out of 2 in 1yj9

Go back to Potassium Binding Sites List in 1yj9
Potassium binding site 2 out of 2 in the Crystal Structure of the Mutant 50S Ribosomal Subunit of Haloarcula Marismortui Containing A Three Residue Deletion in L22


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of the Mutant 50S Ribosomal Subunit of Haloarcula Marismortui Containing A Three Residue Deletion in L22 within 5.0Å range:
probe atom residue distance (Å) B Occ
0:K8402

b:69.0
occ:1.00
O 0:HOH8836 2.9 39.2 1.0
O4 0:U163 2.9 40.5 1.0
O4 0:U172 3.0 45.1 1.0
O 0:HOH8967 3.2 25.9 1.0
OP2 0:C162 3.3 34.2 1.0
O 0:HOH8933 3.3 34.0 1.0
O 0:HOH4751 3.5 51.9 1.0
O 0:HOH7603 3.6 40.9 1.0
CD M:ARG82 3.7 39.7 1.0
C4 0:U172 3.9 44.1 1.0
O 0:HOH9143 3.9 38.6 1.0
C4 0:U163 3.9 39.5 1.0
N3 0:U172 4.0 43.3 1.0
N4 0:C171 4.2 44.4 1.0
NE M:ARG82 4.4 41.4 1.0
C5 0:U163 4.5 40.1 1.0
OP2 0:A169 4.6 40.2 1.0
P 0:C162 4.6 35.9 1.0
O6 0:G164 4.6 37.4 1.0
O 0:HOH7602 4.7 36.5 1.0
OP1 0:A169 4.8 37.0 1.0
CG M:ARG82 4.8 37.3 1.0
MG 0:MG8054 4.9 43.8 1.0
CB M:ARG82 4.9 37.7 1.0
N3 0:C173 4.9 39.7 1.0
OP1 0:C162 5.0 37.0 1.0

Reference:

D.Tu, G.Blaha, P.B.Moore, T.A.Steitz. Structures of Mlsbk Antibiotics Bound to Mutated Large Ribosomal Subunits Provide A Structural Explanation For Resistance. Cell(Cambridge,Mass.) V. 121 257 2005.
ISSN: ISSN 0092-8674
PubMed: 15851032
DOI: 10.1016/J.CELL.2005.02.005
Page generated: Sat Aug 9 02:58:39 2025

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