Zinc in PDB 2cja: Crystal Structure of Methanosarcina Barkeri Seryl-Trna Synthetase Complexed with Atp

All present enzymatic activity of Crystal Structure of Methanosarcina Barkeri Seryl-Trna Synthetase Complexed with Atp:
6.1.1.11;

The structure of Crystal Structure of Methanosarcina Barkeri Seryl-Trna Synthetase Complexed with Atp, PDB code: 2cja was solved by S.Bilokapic, T.Maier, D.Ahel, I.Gruic-Sovulj, D.Soll, I.Weygand-Durasevic, N.Ban, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.74 / 2.2
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	97.314, 97.314, 270.051, 90.00, 90.00, 120.00
R / Rfree (%)	20.3 / 23.3

The structure of Crystal Structure of Methanosarcina Barkeri Seryl-Trna Synthetase Complexed with Atp also contains other interesting chemical elements:

Magnesium	(Mg)	2 atoms
Chlorine	(Cl)	2 atoms

The binding sites of Zinc atom in the Crystal Structure of Methanosarcina Barkeri Seryl-Trna Synthetase Complexed with Atp (pdb code 2cja). 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 Methanosarcina Barkeri Seryl-Trna Synthetase Complexed with Atp, PDB code: 2cja:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Methanosarcina Barkeri Seryl-Trna Synthetase Complexed with Atp


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 Methanosarcina Barkeri Seryl-Trna Synthetase Complexed with Atp within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1503 b:39.6 occ:1.00 OE2 A:GLU355 2.1 62.6 1.0 SG A:CYS306 2.6 64.3 1.0 SG A:CYS461 2.7 64.4 1.0 CD A:GLU355 3.2 61.3 1.0 O A:ALA304 3.5 60.7 1.0 CB A:CYS461 3.5 60.4 1.0 CB A:CYS306 3.6 61.6 1.0 O A:HOH2158 3.6 44.3 1.0 O2B A:ATP1505 3.7 60.7 1.0 OE1 A:GLU355 3.7 60.7 1.0 CG A:GLU355 4.4 58.4 1.0 N A:CYS306 4.4 60.9 1.0 C A:ALA304 4.5 60.5 1.0 CA A:CYS306 4.6 61.8 1.0 CB A:ALA304 4.7 60.0 1.0 O A:HOH2126 4.8 43.9 1.0 CA A:CYS461 4.9 60.4 1.0 O2G A:ATP1505 5.0 64.9 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Methanosarcina Barkeri Seryl-Trna Synthetase Complexed with Atp


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 Methanosarcina Barkeri Seryl-Trna Synthetase Complexed with Atp within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1503 b:44.2 occ:1.00 OE2 B:GLU355 2.1 60.1 1.0 SG B:CYS306 2.6 62.9 1.0 SG B:CYS461 2.7 64.6 1.0 CD B:GLU355 3.1 62.3 1.0 O B:ALA304 3.5 62.2 1.0 CB B:CYS461 3.5 62.7 1.0 O B:HOH2174 3.5 51.4 1.0 CB B:CYS306 3.5 63.0 1.0 OE1 B:GLU355 3.6 60.1 1.0 CG B:GLU355 4.3 60.8 1.0 O B:HOH2231 4.3 54.8 1.0 N B:CYS306 4.4 62.5 1.0 C B:ALA304 4.5 61.9 1.0 CA B:CYS306 4.6 62.7 1.0 O B:HOH2200 4.6 68.3 1.0 CB B:ALA304 4.7 61.2 1.0 O B:HOH2155 4.8 53.4 1.0 CA B:CYS461 4.9 62.6 1.0

S.Bilokapic, T.Maier, D.Ahel, I.Gruic-Sovulj, D.Soll, I.Weygand-Durasevic, N.Ban. Structure of the Unusual Seryl-Trna Synthetase Reveals A Distinct Zinc-Dependent Mode of Substrate Recognition Embo J. V. 25 2498 2006.
ISSN: ISSN 0261-4189
PubMed: 16675947
DOI: 10.1038/SJ.EMBOJ.7601129