Potassium in PDB 1vqn: The Structure of Cc-Hpmn and Cca-Phe-Cap-Bio Bound to the Large Ribosomal Subunit of Haloarcula Marismortui

The structure of The Structure of Cc-Hpmn and Cca-Phe-Cap-Bio Bound to the Large Ribosomal Subunit of Haloarcula Marismortui, PDB code: 1vqn was solved by T.M.Schmeing, T.A.Steitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.40
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	211.721, 298.782, 575.272, 90.00, 90.00, 90.00
R / Rfree (%)	21.2 / 24.8

The structure of The Structure of Cc-Hpmn and Cca-Phe-Cap-Bio Bound to the Large Ribosomal Subunit of Haloarcula Marismortui also contains other interesting chemical elements:

Strontium	(Sr)	114 atoms
Magnesium	(Mg)	94 atoms
Cadmium	(Cd)	5 atoms
Chlorine	(Cl)	22 atoms
Sodium	(Na)	75 atoms

The binding sites of Potassium atom in the The Structure of Cc-Hpmn and Cca-Phe-Cap-Bio Bound to the Large Ribosomal Subunit of Haloarcula Marismortui (pdb code 1vqn). 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 Structure of Cc-Hpmn and Cca-Phe-Cap-Bio Bound to the Large Ribosomal Subunit of Haloarcula Marismortui, PDB code: 1vqn:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the The Structure of Cc-Hpmn and Cca-Phe-Cap-Bio Bound to the Large Ribosomal Subunit of Haloarcula Marismortui


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of The Structure of Cc-Hpmn and Cca-Phe-Cap-Bio Bound to the Large Ribosomal Subunit of Haloarcula Marismortui within 5.0Å range: probe atom residue distance (Å) B Occ 0:K9001 b:74.5 occ:1.00 O6 0:G2482 2.8 37.5 1.0 O6 0:G2102 2.9 47.7 1.0 N7 0:G2482 3.0 38.1 1.0 O4' 0:C2536 3.0 40.0 1.0 O2 0:C2536 3.1 38.8 1.0 N7 0:G2102 3.4 46.7 1.0 C6 0:G2482 3.5 37.1 1.0 C1' 0:C2536 3.5 38.7 1.0 C5 0:G2482 3.5 38.6 1.0 C2 0:C2536 3.6 38.4 1.0 C6 0:G2102 3.6 45.6 1.0 N1 0:C2536 3.8 39.1 1.0 C5 0:G2102 3.8 45.1 1.0 C4' 0:C2536 3.8 40.8 1.0 N6 0:A2486 3.9 44.0 1.0 C8 0:G2482 4.2 38.8 1.0 O2 0:U2535 4.2 52.1 1.0 C5' 0:C2536 4.4 40.6 1.0 N3 0:C2536 4.5 39.7 1.0 C2 0:U2535 4.5 50.0 1.0 C8 0:G2102 4.6 46.4 1.0 C2' 0:U2535 4.6 47.1 1.0 OP1 0:U2539 4.7 55.0 1.0 C6 0:C2536 4.8 37.7 1.0 N1 0:G2482 4.8 39.4 1.0 N1 0:G2102 4.9 46.0 1.0 C4 0:G2482 4.9 38.7 1.0 N3 0:U2535 4.9 48.0 1.0 C2' 0:C2536 5.0 39.6 1.0 O2' 0:U2535 5.0 46.4 1.0 O5' 0:C2536 5.0 44.2 1.0

Potassium binding site 2 out of 2 in the The Structure of Cc-Hpmn and Cca-Phe-Cap-Bio Bound to the Large Ribosomal Subunit of Haloarcula Marismortui


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of The Structure of Cc-Hpmn and Cca-Phe-Cap-Bio Bound to the Large Ribosomal Subunit of Haloarcula Marismortui within 5.0Å range: probe atom residue distance (Å) B Occ 0:K9002 b:88.3 occ:1.00 O4 0:U172 2.7 38.1 1.0 O M:HOH9324 2.9 37.2 1.0 CD M:ARG82 2.9 74.3 1.0 O 0:HOH9642 2.9 38.0 1.0 O 0:HOH9739 3.0 42.0 1.0 O4 0:U163 3.2 35.3 1.0 O 0:HOH5482 3.4 76.8 1.0 NE M:ARG82 3.4 73.8 1.0 OP2 0:C162 3.5 30.2 1.0 C4 0:U172 3.7 35.7 1.0 O 0:HOH8341 3.8 99.5 1.0 N3 0:U172 3.9 36.3 1.0 O 0:HOH9947 4.0 45.2 1.0 O 0:HOH8340 4.1 56.5 1.0 CG M:ARG82 4.2 78.0 1.0 C4 0:U163 4.3 34.7 1.0 N4 0:C171 4.4 40.0 1.0 CZ M:ARG82 4.5 76.1 1.0 OP2 0:A169 4.6 35.5 1.0 CB M:ARG82 4.6 80.3 1.0 O6 0:G164 4.7 33.1 1.0 P 0:C162 4.7 30.9 1.0 OP1 0:A169 4.8 38.1 1.0 C5 0:U163 4.9 34.2 1.0 NH1 M:ARG82 5.0 75.8 1.0

T.M.Schmeing, K.S.Huang, S.A.Strobel, T.A.Steitz. An Induced-Fit Mechanism to Promote Peptide Bond Formation and Exclude Hydrolysis of Peptidyl-Trna. Nature V. 438 520 2005.
ISSN: ISSN 0028-0836
PubMed: 16306996
DOI: 10.1038/NATURE04152