Zinc in PDB 2uu9: Structure of the Thermus Thermophilus 30S Ribosomal Subunit Complexed with A Valine-Asl with CMO5U in Position 34 Bound to An Mrna with A Gug-Codon in the A-Site and Paromomycin.

The structure of Structure of the Thermus Thermophilus 30S Ribosomal Subunit Complexed with A Valine-Asl with CMO5U in Position 34 Bound to An Mrna with A Gug-Codon in the A-Site and Paromomycin., PDB code: 2uu9 was solved by A.Weixlbaumer, F.V.Murphy, A.Dziergowska, A.Malkiewicz, F.A.P.Vendeix, P.F.Agris, V.Ramakrishnan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.89 / 3.10
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	400.943, 400.943, 174.219, 90.00, 90.00, 90.00
R / Rfree (%)	22.8 / 26.8

The structure of Structure of the Thermus Thermophilus 30S Ribosomal Subunit Complexed with A Valine-Asl with CMO5U in Position 34 Bound to An Mrna with A Gug-Codon in the A-Site and Paromomycin. also contains other interesting chemical elements:

Magnesium	(Mg)	161 atoms
Potassium	(K)	36 atoms

The binding sites of Zinc atom in the Structure of the Thermus Thermophilus 30S Ribosomal Subunit Complexed with A Valine-Asl with CMO5U in Position 34 Bound to An Mrna with A Gug-Codon in the A-Site and Paromomycin. (pdb code 2uu9). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of the Thermus Thermophilus 30S Ribosomal Subunit Complexed with A Valine-Asl with CMO5U in Position 34 Bound to An Mrna with A Gug-Codon in the A-Site and Paromomycin., PDB code: 2uu9:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of the Thermus Thermophilus 30S Ribosomal Subunit Complexed with A Valine-Asl with CMO5U in Position 34 Bound to An Mrna with A Gug-Codon in the A-Site and Paromomycin.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the Thermus Thermophilus 30S Ribosomal Subunit Complexed with A Valine-Asl with CMO5U in Position 34 Bound to An Mrna with A Gug-Codon in the A-Site and Paromomycin. within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn301 b:42.5 occ:1.00 SG D:CYS31 2.1 53.0 1.0 SG D:CYS26 2.3 55.2 1.0 SG D:CYS9 2.3 46.7 1.0 SG D:CYS12 2.7 50.7 1.0 O D:CYS31 3.1 70.7 1.0 CB D:CYS31 3.4 63.0 1.0 CA D:CYS31 3.7 67.8 1.0 C D:CYS31 3.8 70.0 1.0 CB D:CYS26 3.8 62.6 1.0 O D:LEU19 3.9 66.8 1.0 CB D:CYS9 4.0 53.2 1.0 CB D:CYS12 4.2 52.8 1.0 CA D:CYS26 4.3 64.8 1.0 CA D:CYS9 4.5 55.0 1.0 CD D:LYS22 4.6 66.5 1.0

Zinc binding site 2 out of 2 in the Structure of the Thermus Thermophilus 30S Ribosomal Subunit Complexed with A Valine-Asl with CMO5U in Position 34 Bound to An Mrna with A Gug-Codon in the A-Site and Paromomycin.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of the Thermus Thermophilus 30S Ribosomal Subunit Complexed with A Valine-Asl with CMO5U in Position 34 Bound to An Mrna with A Gug-Codon in the A-Site and Paromomycin. within 5.0Å range: probe atom residue distance (Å) B Occ N:Zn102 b:55.2 occ:1.00 SG N:CYS27 1.9 49.5 1.0 SG N:CYS43 2.0 44.2 1.0 SG N:CYS40 2.4 51.2 1.0 SG N:CYS24 2.6 60.5 1.0 CB N:CYS27 3.0 51.1 1.0 CB N:CYS40 3.1 53.2 1.0 CB N:CYS43 3.2 44.9 1.0 N N:CYS27 3.6 53.3 1.0 CB N:CYS24 3.7 57.9 1.0 N N:CYS40 3.8 54.6 1.0 CB N:ARG29 3.8 60.2 1.0 CA N:CYS27 3.8 52.9 1.0 CA N:CYS40 4.0 54.2 1.0 N N:CYS43 4.1 48.9 1.0 CA N:CYS43 4.2 46.9 1.0 O N:CYS40 4.4 54.4 1.0 C N:ARG26 4.5 52.6 1.0 N2 A:G1202 4.5 62.6 1.0 C N:CYS27 4.5 53.8 1.0 CB N:ARG26 4.6 50.6 1.0 C N:CYS40 4.6 54.3 1.0 N N:ARG29 4.6 60.4 1.0 CG N:ARG29 4.7 60.1 1.0 N N:GLY28 4.8 56.0 1.0 CG N:ARG26 4.9 49.9 1.0 CA N:ARG29 4.9 60.5 1.0 CA N:ARG26 4.9 52.2 1.0 N3 A:G1202 4.9 61.3 1.0

A.Weixlbaumer, F.V.Murphy 4Th., A.Dziergowska, A.Malkiewicz, F.A.Vendeix, P.F.Agris, V.Ramakrishnan. Mechanism For Expanding the Decoding Capacity of Transfer Rnas By Modification of Uridines. Nat. Struct. Mol. Biol. V. 14 498 2007.
ISSN: ISSN 1545-9993
PubMed: 17496902
DOI: 10.1038/NSMB1242