Chlorine in PDB 6o76: Human Cytosolic Histidyl-Trna Synthetase (Hisrs) with Whep Domain

All present enzymatic activity of Human Cytosolic Histidyl-Trna Synthetase (Hisrs) with Whep Domain:
6.1.1.21;

The structure of Human Cytosolic Histidyl-Trna Synthetase (Hisrs) with Whep Domain, PDB code: 6o76 was solved by B.Kuhle, X.L.Yang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.02 / 2.79
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	97.669, 97.669, 254.409, 90.00, 90.00, 90.00
R / Rfree (%)	23.6 / 29.5

The binding sites of Chlorine atom in the Human Cytosolic Histidyl-Trna Synthetase (Hisrs) with Whep Domain (pdb code 6o76). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Human Cytosolic Histidyl-Trna Synthetase (Hisrs) with Whep Domain, PDB code: 6o76:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Human Cytosolic Histidyl-Trna Synthetase (Hisrs) with Whep Domain


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human Cytosolic Histidyl-Trna Synthetase (Hisrs) with Whep Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl601 b:67.1 occ:1.00 NZ A:LYS240 3.4 71.5 1.0 OG A:SER236 3.8 66.8 1.0 NZ A:LYS257 4.2 65.9 1.0 CB A:SER236 4.3 63.1 1.0 CE A:LYS240 4.4 72.2 1.0 OE2 A:GLU252 4.6 95.2 1.0 CE A:LYS257 4.9 61.4 1.0

Chlorine binding site 2 out of 2 in the Human Cytosolic Histidyl-Trna Synthetase (Hisrs) with Whep Domain


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Human Cytosolic Histidyl-Trna Synthetase (Hisrs) with Whep Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl602 b:63.0 occ:1.00 O B:GLY121 3.7 0.2 1.0 NZ A:LYS60 3.8 1.0 1.0 CA B:GLY122 3.9 0.8 1.0 NH2 A:ARG169 3.9 82.1 1.0 NH1 A:ARG169 4.0 66.0 1.0 C B:GLY121 4.3 0.3 1.0 CD A:LYS60 4.4 94.5 1.0 CE A:LYS60 4.4 99.1 1.0 CZ A:ARG169 4.5 73.6 1.0 N B:GLY122 4.5 0.0 1.0 CZ A:ARG158 5.0 0.0 1.0 NH2 A:ARG158 5.0 0.9 1.0

D.Blocquel, L.Sun, Z.Matuszek, S.Li, T.Weber, B.Kuhle, G.Kooi, N.Wei, J.Baets, T.Pan, P.Schimmel, X.L.Yang. Cmt Disease Severity Correlates with Mutation-Induced Open Conformation of Histidyl-Trna Synthetase, Not Aminoacylation Loss, in Patient Cells. Proc.Natl.Acad.Sci.Usa V. 116 19440 2019.
ISSN: ESSN 1091-6490
PubMed: 31501329
DOI: 10.1073/PNAS.1908288116