Zinc in PDB 1li5: Crystal Structure of Cysteinyl-Trna Synthetase

All present enzymatic activity of Crystal Structure of Cysteinyl-Trna Synthetase:
6.1.1.16;

The structure of Crystal Structure of Cysteinyl-Trna Synthetase, PDB code: 1li5 was solved by K.J.Newberry, Y.-M.Hou, J.J.Perona, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.89 / 2.30
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	119.160, 119.160, 144.300, 90.00, 90.00, 90.00
R / Rfree (%)	24.5 / 28.3

The binding sites of Zinc atom in the Crystal Structure of Cysteinyl-Trna Synthetase (pdb code 1li5). 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 Cysteinyl-Trna Synthetase, PDB code: 1li5:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Cysteinyl-Trna Synthetase


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 Cysteinyl-Trna Synthetase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn963 b:32.3 occ:1.00 NE2 A:HIS234 2.0 28.3 1.0 OE2 A:GLU238 2.3 27.1 1.0 SG A:CYS209 2.3 35.5 1.0 SG A:CYS28 2.6 31.1 1.0 CE1 A:HIS234 2.9 28.1 1.0 CD2 A:HIS234 3.0 27.6 1.0 CB A:CYS209 3.1 28.5 1.0 CD A:GLU238 3.3 28.7 1.0 CB A:CYS28 3.6 30.4 1.0 ND1 A:HIS234 4.0 27.6 1.0 OE1 A:GLU238 4.0 28.6 1.0 CG A:HIS234 4.1 27.9 1.0 CG A:GLU238 4.3 26.4 1.0 CE1 A:HIS235 4.4 27.2 1.0 CE2 A:TYR26 4.4 26.7 1.0 NE2 A:HIS224 4.4 25.6 1.0 CA A:CYS28 4.5 30.0 1.0 CA A:CYS209 4.5 27.3 1.0 ND1 A:HIS235 4.5 27.9 1.0 OH A:TYR26 4.7 25.2 1.0 CE1 A:HIS224 4.8 24.9 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Cysteinyl-Trna Synthetase


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 Cysteinyl-Trna Synthetase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn964 b:36.2 occ:1.00 NE2 B:HIS234 1.8 32.3 1.0 SG B:CYS28 2.1 32.1 1.0 SG B:CYS209 2.3 33.7 1.0 OE2 B:GLU238 2.4 23.6 1.0 CD2 B:HIS234 2.8 31.8 1.0 CE1 B:HIS234 2.8 31.9 1.0 CB B:CYS209 3.2 33.9 1.0 CB B:CYS28 3.4 31.2 1.0 CD B:GLU238 3.5 26.0 1.0 ND1 B:HIS234 3.8 30.6 1.0 CG B:HIS234 3.9 33.2 1.0 OE1 B:GLU238 4.2 28.3 1.0 CA B:CYS28 4.3 30.7 1.0 CG B:GLU238 4.4 26.3 1.0 NE2 B:HIS224 4.5 27.3 1.0 CE2 B:TYR26 4.5 28.3 1.0 CE1 B:HIS235 4.6 29.9 1.0 CA B:CYS209 4.7 36.0 1.0 ND1 B:HIS235 4.7 30.4 1.0 OH B:TYR26 4.7 27.2 1.0 CE1 B:HIS224 4.8 24.2 1.0 OD1 B:ASN66 5.0 40.2 1.0

K.J.Newberry, Y.-M.Hou, J.J.Perona. Structural Origins of Amino Acid Selection Without Editing By Cysteinyl-Trna Synthetase Embo J. V. 21 2778 2002.
ISSN: ISSN 0261-4189
PubMed: 12032090
DOI: 10.1093/EMBOJ/21.11.2778