Zinc in PDB 4cqn: Crystal Structure of the E.Coli Leurs-Trna Complex with the Non-Cognate Isoleucyl Adenylate Analogue

All present enzymatic activity of Crystal Structure of the E.Coli Leurs-Trna Complex with the Non-Cognate Isoleucyl Adenylate Analogue:
6.1.1.4;

The structure of Crystal Structure of the E.Coli Leurs-Trna Complex with the Non-Cognate Isoleucyl Adenylate Analogue, PDB code: 4cqn was solved by A.Palencia, S.Cusack, N.Cvetesic, I.Haslaz, I.Gruic-Sovulj, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.49 / 2.50
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	155.620, 67.580, 224.590, 90.00, 105.00, 90.00
R / Rfree (%)	21.373 / 29.02

The structure of Crystal Structure of the E.Coli Leurs-Trna Complex with the Non-Cognate Isoleucyl Adenylate Analogue also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Zinc atom in the Crystal Structure of the E.Coli Leurs-Trna Complex with the Non-Cognate Isoleucyl Adenylate Analogue (pdb code 4cqn). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the E.Coli Leurs-Trna Complex with the Non-Cognate Isoleucyl Adenylate Analogue, PDB code: 4cqn:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the E.Coli Leurs-Trna Complex with the Non-Cognate Isoleucyl Adenylate Analogue


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the E.Coli Leurs-Trna Complex with the Non-Cognate Isoleucyl Adenylate Analogue within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1861 b:65.7 occ:1.00 OD2 A:ASP162 1.9 76.0 1.0 SG A:CYS159 2.6 60.2 1.0 SG A:CYS176 2.6 58.6 1.0 CG A:ASP162 3.0 78.4 1.0 SG A:CYS179 3.1 84.1 1.0 CB A:CYS176 3.4 57.2 1.0 CG2 A:THR181 3.5 58.1 1.0 O A:HOH2058 3.8 23.4 1.0 CB A:ASP162 3.9 75.1 1.0 OD1 A:ASP162 3.9 80.3 1.0 CB A:CYS159 4.0 52.6 1.0 O A:CYS179 4.2 84.1 1.0 N A:CYS179 4.3 82.3 1.0 NH1 A:ARG178 4.4 80.5 1.0 N A:ASP162 4.4 70.7 1.0 CB A:ARG178 4.4 80.0 1.0 CB A:ASN161 4.6 71.3 1.0 CB A:CYS179 4.7 80.5 1.0 CA A:ASP162 4.8 69.5 1.0 CA A:CYS176 4.8 58.4 1.0 ND2 A:ASN161 4.9 70.9 1.0 CA A:CYS179 4.9 83.7 1.0 CB A:THR181 5.0 57.6 1.0 C A:CYS179 5.0 80.8 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the E.Coli Leurs-Trna Complex with the Non-Cognate Isoleucyl Adenylate Analogue


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the E.Coli Leurs-Trna Complex with the Non-Cognate Isoleucyl Adenylate Analogue within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn1861 b:0.4 occ:1.00 SG D:CYS176 2.4 87.4 1.0 OD2 D:ASP162 2.8 67.9 1.0 SG D:CYS159 2.9 78.2 1.0 SG D:CYS179 3.1 0.1 1.0 OD1 D:ASP162 3.2 73.8 1.0 CG D:ASP162 3.2 74.3 1.0 CB D:ARG178 3.7 0.6 1.0 CB D:CYS176 3.7 88.8 1.0 N D:CYS179 3.8 0.0 1.0 CB D:CYS179 4.3 0.1 1.0 CB D:CYS159 4.4 97.7 1.0 CB D:ASP162 4.4 79.1 1.0 CA D:ARG178 4.4 0.1 1.0 N D:ARG178 4.4 0.6 1.0 CA D:CYS179 4.6 0.2 1.0 C D:ARG178 4.6 0.7 1.0 OG1 D:THR181 4.6 0.0 1.0 ND2 D:ASN161 4.7 0.9 1.0 CG D:ARG178 4.8 0.5 1.0 CB D:ASN161 4.8 0.0 1.0 CB D:THR181 4.8 0.5 1.0 N D:ASP162 4.9 99.4 1.0

N.Cvetesic, A.Palencia, I.Halasz, S.Cusack, I.Gruic-Sovulj. The Physiological Target For Leurs Translational Quality Control Is Norvaline Embo J. V. 33 1639 2014.
ISSN: ISSN 0261-4189
PubMed: 24935946
DOI: 10.15252/EMBJ.201488199