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Potassium in PDB 1kqs: The Haloarcula Marismortui 50S Complexed with A Pretranslocational Intermediate in Protein Synthesis

Protein crystallography data

The structure of The Haloarcula Marismortui 50S Complexed with A Pretranslocational Intermediate in Protein Synthesis, PDB code: 1kqs was solved by T.M.Schmeing, A.C.Seila, J.L.Hansen, B.Freeborn, J.K.Soukup, S.A.Scaringe, S.A.Strobel, 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) 20.00 / 3.10
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 212.784, 300.349, 574.961, 90.00, 90.00, 90.00
R / Rfree (%) 17.3 / 22

Other elements in 1kqs:

The structure of The Haloarcula Marismortui 50S Complexed with A Pretranslocational Intermediate in Protein Synthesis also contains other interesting chemical elements:

Magnesium (Mg) 117 atoms
Cadmium (Cd) 5 atoms
Chlorine (Cl) 22 atoms
Sodium (Na) 86 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the The Haloarcula Marismortui 50S Complexed with A Pretranslocational Intermediate in Protein Synthesis (pdb code 1kqs). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the The Haloarcula Marismortui 50S Complexed with A Pretranslocational Intermediate in Protein Synthesis, PDB code: 1kqs:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 1kqs

Go back to Potassium Binding Sites List in 1kqs
Potassium binding site 1 out of 2 in the The Haloarcula Marismortui 50S Complexed with A Pretranslocational Intermediate in Protein Synthesis


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of The Haloarcula Marismortui 50S Complexed with A Pretranslocational Intermediate in Protein Synthesis within 5.0Å range:
probe atom residue distance (Å) B Occ
0:K8201

b:80.4
occ:1.00
O6 0:G2482 2.7 33.1 1.0
O6 0:G2102 2.8 30.9 1.0
N7 0:G2482 3.0 34.4 1.0
O4' 0:C2536 3.1 27.0 1.0
O2 0:C2536 3.1 27.4 1.0
N7 0:G2102 3.3 28.1 1.0
C6 0:G2482 3.4 31.6 1.0
C6 0:G2102 3.5 29.6 1.0
C5 0:G2482 3.5 32.4 1.0
C1' 0:C2536 3.6 26.3 1.0
C2 0:C2536 3.6 28.3 1.0
C5 0:G2102 3.7 28.6 1.0
N1 0:C2536 3.8 28.0 1.0
C4' 0:C2536 3.9 26.0 1.0
N6 0:A2486 4.0 29.5 1.0
C8 0:G2482 4.3 33.6 1.0
C5' 0:C2536 4.4 26.9 1.0
O2 0:U2535 4.4 36.3 1.0
C8 0:G2102 4.4 28.0 1.0
N3 0:C2536 4.5 29.1 1.0
OP1 0:U2539 4.6 24.8 1.0
C2 0:U2535 4.7 35.2 1.0
C2' 0:U2535 4.7 32.6 1.0
N1 0:G2482 4.7 33.3 1.0
N1 0:G2102 4.8 30.0 1.0
C4 0:G2482 4.8 33.0 1.0
C6 0:C2536 4.9 28.7 1.0
O5' 0:C2536 4.9 28.4 1.0
N3 0:U2535 5.0 33.4 1.0
C2' 0:C2536 5.0 25.6 1.0

Potassium binding site 2 out of 2 in 1kqs

Go back to Potassium Binding Sites List in 1kqs
Potassium binding site 2 out of 2 in the The Haloarcula Marismortui 50S Complexed with A Pretranslocational Intermediate in Protein Synthesis


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of The Haloarcula Marismortui 50S Complexed with A Pretranslocational Intermediate in Protein Synthesis within 5.0Å range:
probe atom residue distance (Å) B Occ
0:K8202

b:69.2
occ:1.00
O 0:HOH8537 2.9 26.9 1.0
O4 0:U172 3.0 29.6 1.0
O4 0:U163 3.0 21.9 1.0
OP2 0:C162 3.1 14.6 1.0
O 0:HOH8630 3.1 49.9 1.0
O 0:HOH8665 3.2 17.4 1.0
O 0:HOH4422 3.3 61.2 1.0
O 0:HOH7305 3.4 25.7 1.0
CD L:ARG82 3.6 0.4 1.0
O 0:HOH8837 3.8 24.7 1.0
C4 0:U172 3.9 29.1 1.0
N3 0:U172 4.0 27.9 1.0
C4 0:U163 4.1 21.2 1.0
O 0:HOH7304 4.2 51.7 1.0
NE L:ARG82 4.2 0.6 1.0
P 0:C162 4.3 16.9 1.0
N4 0:C171 4.5 34.9 1.0
C5 0:U163 4.6 21.4 1.0
OP1 0:C162 4.6 15.8 1.0
OP2 0:A169 4.6 26.1 1.0
MG 0:MG8054 4.7 28.3 1.0
CG L:ARG82 4.8 0.6 1.0
O6 0:G164 4.8 24.3 1.0
OP1 0:A169 4.9 26.8 1.0
CB L:ARG82 4.9 0.3 1.0
N3 0:C173 4.9 18.3 1.0

Reference:

T.M.Schmeing, A.C.Seila, J.L.Hansen, B.Freeborn, J.K.Soukup, S.A.Scaringe, S.A.Strobel, P.B.Moore, T.A.Steitz. A Pre-Translocational Intermediate in Protein Synthesis Observed in Crystals of Enzymatically Active 50S Subunits. Nat.Struct.Biol. V. 9 225 2002.
ISSN: ISSN 1072-8368
PubMed: 11828326
Page generated: Sun Dec 13 22:48:18 2020

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