Chlorine in PDB 2pqt: Human N-Acetyltransferase 1

All present enzymatic activity of Human N-Acetyltransferase 1:
2.3.1.5;

The structure of Human N-Acetyltransferase 1, PDB code: 2pqt was solved by W.Tempel, H.Wu, L.Dombrovski, P.Loppnau, J.Weigelt, M.Sundstrom, C.H.Arrowsmith, A.M.Edwards, D.M.Grant, A.Bochkarev, A.N.Plotnikov, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	22.00 / 1.78
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	37.274, 44.975, 83.959, 90.00, 99.17, 90.00
R / Rfree (%)	17 / 21.6

The binding sites of Chlorine atom in the Human N-Acetyltransferase 1 (pdb code 2pqt). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Human N-Acetyltransferase 1, PDB code: 2pqt:

Chlorine binding site 1 out of 1 in the Human N-Acetyltransferase 1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human N-Acetyltransferase 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:28.7 occ:1.00 NE2 A:GLN133 2.9 24.8 1.0 O A:HOH553 3.0 24.5 1.0 N A:VAL146 3.1 15.4 1.0 CB A:GLN145 3.5 17.1 1.0 CA A:GLN145 3.6 18.0 1.0 CB A:TRP132 3.7 16.3 1.0 CD A:GLN133 3.8 24.0 1.0 C A:GLN145 3.9 17.9 1.0 CG A:GLN133 3.9 18.6 1.0 CG2 A:VAL146 3.9 18.5 1.0 CB A:VAL146 4.0 18.8 1.0 CG A:GLN145 4.0 16.4 1.0 CA A:VAL146 4.1 16.8 1.0 CE3 A:TRP132 4.3 17.6 1.0 CD A:PRO147 4.4 15.7 1.0 OE1 A:GLN145 4.5 15.5 1.0 CD A:GLN145 4.5 16.8 1.0 CG A:TRP132 4.6 16.4 1.0 O A:HOH575 4.7 30.3 1.0 C A:TRP132 4.7 18.0 1.0 CA A:TRP132 4.7 15.7 1.0 CD2 A:TRP132 4.8 15.5 1.0 N A:GLN133 4.9 17.5 1.0 CB A:GLN133 4.9 17.2 1.0 OE1 A:GLN133 4.9 30.0 1.0

H.Wu, L.Dombrovsky, W.Tempel, F.Martin, P.Loppnau, G.H.Goodfellow, D.M.Grant, A.N.Plotnikov. Structural Basis of Substrate-Binding Specificity of Human Arylamine N-Acetyltransferases. J.Biol.Chem. V. 282 30189 2007.
ISSN: ISSN 0021-9258
PubMed: 17656365
DOI: 10.1074/JBC.M704138200