Chlorine in PDB 3w6x: Yeast N-Acetyltransferase MPR1 in Complex with Chop

The structure of Yeast N-Acetyltransferase MPR1 in Complex with Chop, PDB code: 3w6x was solved by R.Nasuno, Y.Hirano, T.Itoh, T.Hakoshima, T.Hibi, H.Takagi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	56.95 / 2.30
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	80.345, 229.340, 84.755, 90.00, 90.94, 90.00
R / Rfree (%)	16.6 / 21.4

The binding sites of Chlorine atom in the Yeast N-Acetyltransferase MPR1 in Complex with Chop (pdb code 3w6x). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Yeast N-Acetyltransferase MPR1 in Complex with Chop, PDB code: 3w6x:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Yeast N-Acetyltransferase MPR1 in Complex with Chop


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Yeast N-Acetyltransferase MPR1 in Complex with Chop within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl302 b:42.7 occ:1.00 N D:LEU78 3.2 30.2 1.0 N D:HIS79 3.2 32.8 1.0 CG C:PRO128 3.5 28.9 1.0 CD C:PRO128 3.9 28.4 1.0 CA D:LEU78 3.9 29.4 1.0 CA D:GLN77 4.0 32.5 1.0 CB D:LEU78 4.0 29.7 1.0 C D:GLN77 4.1 32.8 1.0 C D:LEU78 4.1 29.9 1.0 CB D:HIS79 4.1 41.3 1.0 CA D:HIS79 4.1 33.8 1.0 O D:HIS79 4.1 30.3 1.0 CB D:GLN77 4.2 34.1 1.0 CD2 D:HIS79 4.3 49.1 1.0 CB C:PRO128 4.4 29.6 1.0 CG D:GLN77 4.4 35.8 1.0 CG D:HIS79 4.5 46.3 1.0 C D:HIS79 4.6 30.2 1.0

Chlorine binding site 2 out of 4 in the Yeast N-Acetyltransferase MPR1 in Complex with Chop


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Yeast N-Acetyltransferase MPR1 in Complex with Chop within 5.0Å range: probe atom residue distance (Å) B Occ E:Cl302 b:39.6 occ:1.00 N E:LEU78 3.2 28.8 1.0 N E:HIS79 3.3 33.3 1.0 CG F:PRO128 3.6 33.4 1.0 CD F:PRO128 3.9 33.2 1.0 CA E:LEU78 3.9 28.4 1.0 CB E:LEU78 4.0 26.0 1.0 CB E:HIS79 4.0 41.0 1.0 CA E:GLN77 4.1 28.5 1.0 C E:GLN77 4.1 30.1 1.0 O E:HIS79 4.1 29.1 1.0 CA E:HIS79 4.1 32.9 1.0 C E:LEU78 4.1 31.5 1.0 CD2 E:HIS79 4.2 47.3 1.0 CB E:GLN77 4.2 30.2 1.0 CG E:HIS79 4.3 45.5 1.0 CB F:PRO128 4.4 33.6 1.0 CG E:GLN77 4.5 33.5 1.0 C E:HIS79 4.6 30.2 1.0

Chlorine binding site 3 out of 4 in the Yeast N-Acetyltransferase MPR1 in Complex with Chop


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Yeast N-Acetyltransferase MPR1 in Complex with Chop within 5.0Å range: probe atom residue distance (Å) B Occ G:Cl302 b:45.2 occ:1.00 N G:LEU78 3.1 37.2 1.0 N G:HIS79 3.3 40.2 1.0 CG H:PRO128 3.6 42.7 1.0 CD H:PRO128 3.8 42.0 1.0 CA G:LEU78 3.9 37.4 1.0 CB G:LEU78 3.9 36.9 1.0 CA G:GLN77 3.9 40.7 1.0 C G:GLN77 4.0 40.2 1.0 C G:LEU78 4.1 38.5 1.0 CB G:GLN77 4.1 41.5 1.0 CB G:HIS79 4.2 46.9 1.0 CA G:HIS79 4.2 41.9 1.0 O G:HIS79 4.2 37.6 1.0 CG G:GLN77 4.4 42.5 1.0 CB H:PRO128 4.4 42.0 1.0 CD2 G:HIS79 4.5 54.5 1.0 CG G:HIS79 4.6 52.4 1.0 C G:HIS79 4.7 38.0 1.0

Chlorine binding site 4 out of 4 in the Yeast N-Acetyltransferase MPR1 in Complex with Chop


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Yeast N-Acetyltransferase MPR1 in Complex with Chop within 5.0Å range: probe atom residue distance (Å) B Occ H:Cl302 b:42.2 occ:1.00 O H:HOH438 2.8 40.4 1.0 N H:LEU78 3.1 32.8 1.0 N H:HIS79 3.3 38.3 1.0 CG G:PRO128 3.5 30.3 1.0 CD G:PRO128 3.6 30.2 1.0 CA H:GLN77 3.9 35.2 1.0 CA H:LEU78 3.9 35.0 1.0 C H:GLN77 4.0 32.2 1.0 CB H:LEU78 4.0 36.2 1.0 CB H:GLN77 4.0 39.0 1.0 C H:LEU78 4.1 36.5 1.0 CB H:HIS79 4.1 44.0 1.0 O H:HIS79 4.2 37.6 1.0 CA H:HIS79 4.2 39.5 1.0 CD2 H:HIS79 4.2 55.6 1.0 CG H:GLN77 4.3 42.5 1.0 CG H:HIS79 4.5 51.9 1.0 CB G:PRO128 4.5 31.8 1.0 C H:HIS79 4.6 37.8 1.0 N G:PRO128 4.9 32.2 1.0

R.Nasuno, Y.Hirano, T.Itoh, T.Hakoshima, T.Hibi, H.Takagi. Structural and Functional Analysis of the Yeast N-Acetyltransferase MPR1 Involved in Oxidative Stress Tolerance Via Proline Metabolism Proc.Natl.Acad.Sci.Usa V. 110 11821 2013.
ISSN: ISSN 0027-8424
PubMed: 23818613
DOI: 10.1073/PNAS.1300558110