Zinc in PDB 1obc: Leucyl-Trna Synthetase From Thermus Thermophilus Complexed with A Post-Transfer Editing Substrate Analogue

The structure of Leucyl-Trna Synthetase From Thermus Thermophilus Complexed with A Post-Transfer Editing Substrate Analogue, PDB code: 1obc was solved by S.Cusack, A.Yaremchuk, M.Tukalo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.65 / 2.10
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	101.896, 154.810, 175.118, 90.00, 90.00, 90.00
R / Rfree (%)	19.3 / 22.5

The binding sites of Zinc atom in the Leucyl-Trna Synthetase From Thermus Thermophilus Complexed with A Post-Transfer Editing Substrate Analogue (pdb code 1obc). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Leucyl-Trna Synthetase From Thermus Thermophilus Complexed with A Post-Transfer Editing Substrate Analogue, PDB code: 1obc:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Leucyl-Trna Synthetase From Thermus Thermophilus Complexed with A Post-Transfer Editing Substrate Analogue


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Leucyl-Trna Synthetase From Thermus Thermophilus Complexed with A Post-Transfer Editing Substrate Analogue within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1812 b:51.5 occ:1.00 SG A:CYS439 2.3 46.7 1.0 SG A:CYS487 2.3 53.0 1.0 SG A:CYS484 2.3 47.8 1.0 SG A:CYS442 2.4 50.7 1.0 CB A:CYS484 3.1 46.2 1.0 CB A:CYS439 3.2 43.2 1.0 CB A:CYS487 3.2 50.8 1.0 CB A:CYS442 3.2 43.6 1.0 N A:CYS487 3.6 50.6 1.0 N A:CYS442 3.8 42.3 1.0 CA A:CYS487 4.0 51.5 1.0 CA A:CYS442 4.2 41.9 1.0 CB A:LYS486 4.5 50.9 1.0 CA A:CYS484 4.6 46.8 1.0 CB A:ALA441 4.6 39.5 1.0 N A:GLY488 4.6 51.3 1.0 CA A:CYS439 4.6 41.1 1.0 C A:LYS486 4.7 50.6 1.0 C A:CYS487 4.8 51.5 1.0 C A:ALA441 4.8 42.1 1.0 N A:ALA441 5.0 41.0 1.0 CA A:LYS486 5.0 49.9 1.0

Zinc binding site 2 out of 2 in the Leucyl-Trna Synthetase From Thermus Thermophilus Complexed with A Post-Transfer Editing Substrate Analogue


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Leucyl-Trna Synthetase From Thermus Thermophilus Complexed with A Post-Transfer Editing Substrate Analogue within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1813 b:32.5 occ:1.00 ND1 A:HIS179 2.1 33.8 1.0 SG A:CYS162 2.3 29.4 1.0 SG A:CYS176 2.3 30.2 1.0 SG A:CYS159 2.3 33.3 1.0 CE1 A:HIS179 2.8 31.4 1.0 CB A:CYS176 3.3 32.2 1.0 CG A:HIS179 3.3 35.4 1.0 CB A:CYS162 3.3 33.5 1.0 CB A:CYS159 3.4 32.6 1.0 N A:CYS162 3.7 33.8 1.0 CB A:HIS179 3.9 35.0 1.0 CA A:CYS162 4.1 32.1 1.0 NE2 A:HIS179 4.1 31.7 1.0 N A:HIS179 4.2 37.1 1.0 CD2 A:HIS179 4.3 33.3 1.0 CB A:ARG178 4.3 37.0 1.0 CB A:LYS161 4.5 39.8 1.0 C A:LYS161 4.6 34.4 1.0 CA A:HIS179 4.7 38.3 1.0 CA A:CYS176 4.7 33.6 1.0 CA A:CYS159 4.8 33.6 1.0 C A:ARG178 4.8 37.9 1.0 N A:ARG178 4.9 35.2 1.0 CA A:ARG178 4.9 36.4 1.0 CA A:LYS161 5.0 36.0 1.0 CD1 A:LEU166 5.0 28.7 1.0

T.Lincecum, M.Tukalo, A.Yaremchuk, R.Mursinna, A.Williams, B.Sproat, W.Van Den Eynde, A.Link, S.Van Calenbergh, M.Grotli, S.Martinis, S.Cusack. Structural and Mechanistic Basis of Pre- and Posttransfer Editing By Leucyl-Trna Synthetase Mol.Cell V. 11 951 2003.
ISSN: ISSN 1097-2765
PubMed: 12718881
DOI: 10.1016/S1097-2765(03)00098-4