Chlorine in PDB 5tjh: Hugdh A136M Substitution

All present enzymatic activity of Hugdh A136M Substitution:
1.1.1.22;

The structure of Hugdh A136M Substitution, PDB code: 5tjh was solved by N.R.Beattie, Z.A.Wood, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.17 / 2.05
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	92.350, 104.590, 107.710, 64.82, 68.35, 73.72
R / Rfree (%)	17.1 / 20.3

The binding sites of Chlorine atom in the Hugdh A136M Substitution (pdb code 5tjh). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Hugdh A136M Substitution, PDB code: 5tjh:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Hugdh A136M Substitution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Hugdh A136M Substitution within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl502 b:78.5 occ:1.00 O B:HOH653 3.5 42.6 1.0 OG B:SER316 3.5 47.9 1.0 CD1 B:TYR356 4.0 48.8 1.0 CG A:MET98 4.1 86.3 1.0 CG B:TYR356 4.2 39.6 1.0 SD A:MET98 4.3 94.2 1.0 O B:ARG312 4.3 34.2 1.0 CB B:TYR356 4.4 42.6 1.0 CG B:ARG312 4.4 46.3 1.0 CE1 B:TYR356 4.5 54.9 1.0 CB B:ALA315 4.5 35.5 1.0 N B:SER316 4.7 37.3 1.0 CB B:SER316 4.8 38.6 1.0 CD2 B:TYR356 4.8 39.5 1.0 CD1 B:ILE319 4.8 48.3 1.0 CA B:SER316 4.9 39.4 1.0

Chlorine binding site 2 out of 2 in the Hugdh A136M Substitution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Hugdh A136M Substitution within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl502 b:56.5 occ:1.00 O D:HOH659 3.3 42.6 1.0 N D:MET419 3.4 49.5 1.0 CE3 D:TRP417 3.6 40.1 1.0 N D:ASP418 3.6 43.2 1.0 CB D:MET419 3.7 45.6 1.0 CG D:MET419 3.7 48.7 1.0 CB D:TRP417 3.9 45.6 1.0 CA D:MET419 4.1 45.2 1.0 CB D:ASP418 4.2 55.9 1.0 C D:TRP417 4.2 44.9 1.0 CA D:ASP418 4.2 47.9 1.0 C D:ASP418 4.2 50.7 1.0 CD2 D:TRP417 4.3 37.7 1.0 SD D:MET419 4.3 52.2 1.0 CA D:TRP417 4.4 48.1 1.0 CZ3 D:TRP417 4.4 41.6 1.0 CG D:TRP417 4.6 38.6 1.0 O D:HOH684 4.8 60.0 1.0 CG D:ASP418 4.9 62.9 1.0 OD2 D:ASP418 5.0 67.2 1.0

N.R.Beattie, N.D.Keul, A.M.Sidlo, Z.A.Wood. Allostery and Hysteresis Are Coupled in Human Udp-Glucose Dehydrogenase. Biochemistry V. 56 202 2017.
ISSN: ISSN 1520-4995
PubMed: 27966912
DOI: 10.1021/ACS.BIOCHEM.6B01044