Chlorine in PDB 1wyd: Crystal Structure of Aspartyl-Trna Synthetase From Sulfolobus Tokodaii

The structure of Crystal Structure of Aspartyl-Trna Synthetase From Sulfolobus Tokodaii, PDB code: 1wyd was solved by Y.Maeda, M.T.Hossain, S.Ubukata, K.Suzuki, T.Sekiguchi, A.Takenaka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.30
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	116.300, 139.250, 75.300, 90.00, 90.00, 90.00
R / Rfree (%)	23.2 / 27.9

The binding sites of Chlorine atom in the Crystal Structure of Aspartyl-Trna Synthetase From Sulfolobus Tokodaii (pdb code 1wyd). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Aspartyl-Trna Synthetase From Sulfolobus Tokodaii, PDB code: 1wyd:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Aspartyl-Trna Synthetase From Sulfolobus Tokodaii


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Aspartyl-Trna Synthetase From Sulfolobus Tokodaii within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl431 b:73.4 occ:1.00 O A:HOH1038 2.9 43.5 1.0 NE2 A:GLN186 3.0 46.5 1.0 N A:THR166 3.1 66.0 1.0 N A:GLU167 3.4 70.1 1.0 CB A:ALA165 3.8 62.7 1.0 CA A:ALA165 3.8 63.2 1.0 CB A:THR166 3.9 67.2 1.0 CG A:GLN186 3.9 43.8 1.0 CA A:THR166 3.9 67.2 1.0 C A:ALA165 3.9 64.6 1.0 CD A:GLN186 3.9 47.8 1.0 O A:GLU167 4.0 72.0 1.0 CD2 A:LEU172 4.1 38.0 1.0 CB A:GLU167 4.2 71.7 1.0 C A:THR166 4.2 68.6 1.0 CD1 A:LEU172 4.2 36.8 1.0 CA A:GLU167 4.3 71.4 1.0 OG1 A:THR166 4.5 65.9 1.0 C A:GLU167 4.6 71.5 1.0 CB A:ALA170 4.8 61.2 1.0 CG A:LEU172 4.8 42.2 1.0 CB A:GLN186 4.9 43.0 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Aspartyl-Trna Synthetase From Sulfolobus Tokodaii


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Aspartyl-Trna Synthetase From Sulfolobus Tokodaii within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl430 b:59.0 occ:1.00 NE2 B:GLN186 2.9 35.9 1.0 N B:THR166 2.9 60.4 1.0 N B:GLU167 3.3 64.0 1.0 O B:HOH1057 3.3 38.5 1.0 CA B:THR166 3.7 61.4 1.0 CB B:THR166 3.7 61.2 1.0 CB B:ALA165 3.8 57.6 1.0 CD B:GLN186 3.8 36.1 1.0 C B:ALA165 3.8 59.0 1.0 CG B:GLN186 3.8 34.3 1.0 CA B:ALA165 3.9 57.4 1.0 C B:THR166 4.0 62.6 1.0 O B:HOH1131 4.1 50.1 1.0 O B:GLU167 4.2 66.4 1.0 CD2 B:LEU172 4.3 47.2 1.0 CA B:GLU167 4.3 66.1 1.0 CB B:ALA170 4.5 60.5 1.0 C B:GLU167 4.6 66.2 1.0 CB B:GLU167 4.6 66.8 1.0 OG1 B:THR166 4.7 61.6 1.0 CD1 B:LEU172 4.7 44.9 1.0 CG2 B:THR166 4.8 60.8 1.0 CG B:GLU167 4.8 69.0 1.0 OE2 B:GLU167 4.9 73.0 1.0 CB B:GLN186 4.9 33.7 1.0 OE1 B:GLN186 4.9 38.9 1.0 O B:ALA165 5.0 59.4 1.0

Y.Sato, Y.Maeda, S.Shimizu, M.T.Hossain, S.Ubukata, K.Suzuki, T.Sekiguchi, A.Takenaka. Structure of the Nondiscriminating Aspartyl-Trna Synthetase From the Crenarchaeon Sulfolobus Tokodaii Strain 7 Reveals the Recognition Mechanism For Two Different Trna Anticodons Acta Crystallogr.,Sect.D V. 63 1042 2007.
ISSN: ISSN 0907-4449
PubMed: 17881821
DOI: 10.1107/S0907444907038292