Zinc in PDB 1nyq: Structure of Staphylococcus Aureus Threonyl-Trna Synthetase Complexed with An Analogue of Threonyl Adenylate

All present enzymatic activity of Structure of Staphylococcus Aureus Threonyl-Trna Synthetase Complexed with An Analogue of Threonyl Adenylate:
6.1.1.3;

The structure of Structure of Staphylococcus Aureus Threonyl-Trna Synthetase Complexed with An Analogue of Threonyl Adenylate, PDB code: 1nyq was solved by A.Torres-Larios, R.Sankaranarayanan, B.Rees, A.C.Dock-Bregeon, D.Moras, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 3.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	104.278, 122.730, 149.941, 90.00, 90.00, 90.00
R / Rfree (%)	20.5 / 28.5

The binding sites of Zinc atom in the Structure of Staphylococcus Aureus Threonyl-Trna Synthetase Complexed with An Analogue of Threonyl Adenylate (pdb code 1nyq). 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 Staphylococcus Aureus Threonyl-Trna Synthetase Complexed with An Analogue of Threonyl Adenylate, PDB code: 1nyq:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of Staphylococcus Aureus Threonyl-Trna Synthetase Complexed with An Analogue of Threonyl Adenylate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Staphylococcus Aureus Threonyl-Trna Synthetase Complexed with An Analogue of Threonyl Adenylate within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1001 b:40.7 occ:1.00 ND1 A:HIS517 2.0 38.2 1.0 NE2 A:HIS387 2.1 29.7 1.0 N A:TSB1002 2.1 37.7 1.0 SG A:CYS336 2.2 49.6 1.0 OG1 A:TSB1002 2.3 37.0 1.0 CD2 A:HIS387 2.9 30.1 1.0 CE1 A:HIS517 2.9 36.8 1.0 CA A:TSB1002 3.0 37.9 1.0 CG A:HIS517 3.0 35.9 1.0 CB A:TSB1002 3.1 35.8 1.0 CE1 A:HIS387 3.3 31.3 1.0 CB A:CYS336 3.3 42.8 1.0 CB A:HIS517 3.5 33.5 1.0 CA A:CYS336 3.9 41.3 1.0 N A:CYS336 3.9 41.6 1.0 NE2 A:HIS517 4.0 37.5 1.0 OH A:TYR468 4.0 51.7 1.0 CD2 A:HIS517 4.1 36.3 1.0 CG A:HIS387 4.1 31.6 1.0 O A:HOH1005 4.1 22.2 1.0 ND1 A:HIS387 4.3 29.6 1.0 C A:TSB1002 4.5 38.4 1.0 CG2 A:TSB1002 4.5 34.4 1.0 OD2 A:ASP385 4.6 22.0 1.0 OD1 A:ASP385 4.6 24.1 1.0 CZ A:TYR468 4.6 50.5 1.0 SD A:MET334 4.7 44.9 1.0 CA A:HIS517 4.7 33.6 1.0 O A:TSB1002 5.0 40.6 1.0 NE2 A:GLN490 5.0 39.5 1.0

Zinc binding site 2 out of 2 in the Structure of Staphylococcus Aureus Threonyl-Trna Synthetase Complexed with An Analogue of Threonyl Adenylate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Staphylococcus Aureus Threonyl-Trna Synthetase Complexed with An Analogue of Threonyl Adenylate within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn2001 b:52.6 occ:1.00 OG1 B:TSB2002 1.7 45.7 1.0 NE2 B:HIS387 2.0 44.6 1.0 SG B:CYS336 2.1 42.0 1.0 ND1 B:HIS517 2.3 43.3 1.0 N B:TSB2002 2.5 41.6 1.0 CB B:TSB2002 2.8 42.9 1.0 CD2 B:HIS387 2.9 44.5 1.0 CA B:TSB2002 3.1 43.3 1.0 CE1 B:HIS517 3.1 43.2 1.0 CE1 B:HIS387 3.1 45.9 1.0 CB B:CYS336 3.3 40.6 1.0 CG B:HIS517 3.4 43.9 1.0 CB B:HIS517 3.9 44.7 1.0 CA B:CYS336 4.0 42.5 1.0 N B:CYS336 4.0 43.0 1.0 CG B:HIS387 4.1 44.7 1.0 CG2 B:TSB2002 4.1 41.1 1.0 ND1 B:HIS387 4.1 44.9 1.0 NE2 B:HIS517 4.2 42.6 1.0 O B:HOH2011 4.3 28.5 1.0 OD2 B:ASP385 4.4 40.5 1.0 OH B:TYR468 4.4 51.3 1.0 CD2 B:HIS517 4.4 43.6 1.0 OD1 B:ASP385 4.4 40.4 1.0 C B:TSB2002 4.6 44.5 1.0 CZ B:TYR468 4.6 51.0 1.0 SD B:MET334 4.8 34.3 1.0 CG B:ASP385 4.8 39.5 1.0 CE2 B:TYR468 4.9 51.8 1.0 CA B:HIS517 5.0 48.0 1.0 CB B:MET334 5.0 40.2 1.0 OE1 B:GLN490 5.0 42.0 1.0

A.Torres-Larios, R.Sankaranarayanan, B.Rees, A.C.Dock-Bregeon, D.Moras. Conformational Movements and Cooperativity Upon Amino Acid, Atp and Trna Binding in Threonyl-Trna Synthetase J.Mol.Biol. V. 331 201 2003.
ISSN: ISSN 0022-2836
PubMed: 12875846
DOI: 10.1016/S0022-2836(03)00719-8