Chlorine in PDB 2azt: Crystal Structure of H176N Mutant of Human Glycine N-Methyltransferase

All present enzymatic activity of Crystal Structure of H176N Mutant of Human Glycine N-Methyltransferase:
2.1.1.20;

The structure of Crystal Structure of H176N Mutant of Human Glycine N-Methyltransferase, PDB code: 2azt was solved by Z.Luka, S.Pakhomova, Y.Luka, M.E.Newcomer, C.Wagner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	13.00 / 2.70
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	76.116, 83.279, 115.450, 90.00, 90.00, 90.00
R / Rfree (%)	23.6 / 28.2

The binding sites of Chlorine atom in the Crystal Structure of H176N Mutant of Human Glycine N-Methyltransferase (pdb code 2azt). 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 Crystal Structure of H176N Mutant of Human Glycine N-Methyltransferase, PDB code: 2azt:

Chlorine binding site 1 out of 1 in the Crystal Structure of H176N Mutant of Human Glycine N-Methyltransferase


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 H176N Mutant of Human Glycine N-Methyltransferase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl3000 b:65.9 occ:1.00 OE1 B:GLN58 3.3 30.2 1.0 CE1 B:PHE79 3.7 21.2 1.0 CZ B:PHE79 3.9 20.6 1.0 CD1 B:PHE79 4.0 23.2 1.0 O B:HOH3030 4.1 55.5 1.0 O B:GLU77 4.1 26.1 1.0 O B:GLY78 4.3 23.9 1.0 CE2 B:PHE79 4.3 21.0 1.0 CD B:GLN58 4.4 28.9 1.0 C B:GLY78 4.4 24.6 1.0 NE B:ARG53 4.4 27.1 1.0 CG B:PHE79 4.5 25.0 1.0 NH2 B:ARG53 4.6 16.6 1.0 O B:CYS57 4.6 26.1 1.0 CD2 B:PHE79 4.6 25.7 1.0 N B:PHE79 4.7 23.3 1.0 NE2 B:GLN58 4.8 23.6 1.0 CA B:GLY78 4.8 24.2 1.0 CA B:PHE79 4.9 23.3 1.0

Z.Luka, S.Pakhomova, Y.Luka, M.E.Newcomer, C.Wagner. Destabilization of Human Glycine N-Methyltransferase By H176N Mutation. Protein Sci. V. 16 1957 2007.
ISSN: ISSN 0961-8368
PubMed: 17660255
DOI: 10.1110/PS.072921507