Zinc in PDB 1n36: Structure of the Thermus Thermophilus 30S Ribosomal Subunit in the Presence of Crystallographically Disordered Codon and Near-Cognate Transfer Rna Anticodon Stem-Loop Mismatched at the Second Codon Position

The structure of Structure of the Thermus Thermophilus 30S Ribosomal Subunit in the Presence of Crystallographically Disordered Codon and Near-Cognate Transfer Rna Anticodon Stem-Loop Mismatched at the Second Codon Position, PDB code: 1n36 was solved by J.M.Ogle, F.V.Murphy Iv, M.J.Tarry, V.Ramakrishnan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	141.42 / 3.65
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	402.836, 402.836, 174.275, 90.00, 90.00, 90.00
R / Rfree (%)	26 / 32.4

The binding sites of Zinc atom in the Structure of the Thermus Thermophilus 30S Ribosomal Subunit in the Presence of Crystallographically Disordered Codon and Near-Cognate Transfer Rna Anticodon Stem-Loop Mismatched at the Second Codon Position (pdb code 1n36). 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 in the Presence of Crystallographically Disordered Codon and Near-Cognate Transfer Rna Anticodon Stem-Loop Mismatched at the Second Codon Position, PDB code: 1n36:
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 in the Presence of Crystallographically Disordered Codon and Near-Cognate Transfer Rna Anticodon Stem-Loop Mismatched at the Second Codon Position


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 in the Presence of Crystallographically Disordered Codon and Near-Cognate Transfer Rna Anticodon Stem-Loop Mismatched at the Second Codon Position within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn306 b:74.6 occ:2.71 CD D:LYS22 2.0 9.1 1.0 SG D:CYS26 2.4 30.1 1.0 SG D:CYS9 2.6 0.9 1.0 SG D:CYS31 2.7 0.6 1.0 CG D:LYS22 2.9 9.1 1.0 CE D:LYS22 3.0 9.1 1.0 NZ D:LYS22 3.1 9.1 1.0 O D:CYS31 3.3 81.5 1.0 CA D:CYS31 3.5 81.5 1.0 CB D:CYS31 3.5 0.6 1.0 O D:LEU19 3.6 69.0 1.0 CB D:LYS22 3.6 9.1 1.0 C D:CYS31 3.7 81.5 1.0 SG D:CYS12 3.7 0.0 1.0 CB D:CYS9 3.8 0.9 1.0 CB D:CYS26 4.1 30.1 1.0 CA D:CYS9 4.1 81.1 1.0 CA D:CYS26 4.6 0.7 1.0 C D:LEU19 4.7 69.0 1.0 N D:CYS31 4.8 81.5 1.0 N D:ALA32 4.9 0.4 1.0 CB D:CYS12 4.9 0.0 1.0

Zinc binding site 2 out of 2 in the Structure of the Thermus Thermophilus 30S Ribosomal Subunit in the Presence of Crystallographically Disordered Codon and Near-Cognate Transfer Rna Anticodon Stem-Loop Mismatched at the Second Codon Position


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 in the Presence of Crystallographically Disordered Codon and Near-Cognate Transfer Rna Anticodon Stem-Loop Mismatched at the Second Codon Position within 5.0Å range: probe atom residue distance (Å) B Occ N:Zn307 b:74.6 occ:1.12 CB N:CYS27 2.0 96.2 1.0 SG N:CYS43 2.2 0.7 1.0 N N:CYS27 2.6 26.4 1.0 CA N:CYS27 2.6 26.4 1.0 SG N:CYS24 2.8 82.6 1.0 CB N:CYS40 3.0 45.0 1.0 N2 A:G1202 3.1 0.4 1.0 CG N:ARG26 3.3 93.9 1.0 SG N:CYS27 3.6 96.2 1.0 C N:ARG26 3.9 0.4 1.0 CD N:ARG26 3.9 93.9 1.0 CB N:CYS43 3.9 0.7 1.0 C N:CYS27 4.0 26.4 1.0 SG N:CYS40 4.0 45.0 1.0 N N:CYS40 4.1 62.4 1.0 CA N:CYS40 4.2 62.4 1.0 C2 A:G1202 4.2 0.4 1.0 CB N:CYS24 4.2 82.6 1.0 N N:CYS43 4.3 43.0 1.0 CB N:ARG26 4.4 93.9 1.0 N3 A:G1202 4.4 0.4 1.0 N N:GLY28 4.4 93.7 1.0 CA N:CYS43 4.5 43.0 1.0 CA N:ARG26 4.5 0.4 1.0 CB N:ILE42 4.8 88.5 1.0 N N:ARG26 4.8 0.4 1.0 O N:ARG26 4.8 0.4 1.0 CD1 N:ILE42 4.9 88.5 1.0 C N:CYS40 4.9 62.4 1.0 O N:CYS27 5.0 26.4 1.0

J.M.Ogle, F.V.Murphy Iv, M.J.Tarry, V.Ramakrishnan. Selection of Trna By the Ribosome Requires A Transition From An Open to A Closed Form Cell(Cambridge,Mass.) V. 111 721 2002.
ISSN: ISSN 0092-8674
PubMed: 12464183
DOI: 10.1016/S0092-8674(02)01086-3