Chlorine in PDB 1e6c: K15M Mutant of Shikimate Kinase From Erwinia Chrysanthemi

All present enzymatic activity of K15M Mutant of Shikimate Kinase From Erwinia Chrysanthemi:
2.7.1.71;

The structure of K15M Mutant of Shikimate Kinase From Erwinia Chrysanthemi, PDB code: 1e6c was solved by J.Maclean, T.Krell, J.R.Coggins, A.J.Lapthorn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.0 / 1.8
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.860, 106.940, 42.750, 90.00, 119.96, 90.00
R / Rfree (%)	18.8 / 22.7

The binding sites of Chlorine atom in the K15M Mutant of Shikimate Kinase From Erwinia Chrysanthemi (pdb code 1e6c). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the K15M Mutant of Shikimate Kinase From Erwinia Chrysanthemi, PDB code: 1e6c:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the K15M Mutant of Shikimate Kinase From Erwinia Chrysanthemi


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of K15M Mutant of Shikimate Kinase From Erwinia Chrysanthemi within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl804 b:20.2 occ:1.00 O2 A:MRD903 3.1 26.4 1.0 CM A:MRD903 3.2 31.2 1.0 N A:ARG11 3.3 17.5 1.0 NH1 A:ARG139 3.4 10.9 1.0 O A:HOH2012 3.4 40.9 1.0 C2 A:MRD903 3.6 29.3 1.0 CA A:GLY79 3.7 14.2 1.0 CB B:SER114 3.8 18.4 1.0 CA A:ALA10 3.8 14.6 1.0 CB A:ALA10 3.9 13.5 1.0 C A:ALA10 4.1 16.3 1.0 C1 A:MRD903 4.1 30.0 1.0 CG A:ARG11 4.1 22.6 1.0 CB A:ARG11 4.1 21.8 1.0 CZ A:ARG139 4.3 12.3 1.0 CA A:ARG11 4.3 19.4 1.0 OG B:SER114 4.3 21.8 1.0 N A:GLY79 4.3 15.7 1.0 NH2 A:ARG139 4.4 13.1 1.0 C A:GLY79 4.6 14.8 1.0 O A:ARG11 4.8 19.8 1.0 OH A:TYR143 4.8 13.8 1.0 O A:HOH2031 4.8 18.4 1.0 O4 A:MRD903 4.9 27.7 1.0 CA B:SER114 5.0 14.3 1.0

Chlorine binding site 2 out of 2 in the K15M Mutant of Shikimate Kinase From Erwinia Chrysanthemi


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of K15M Mutant of Shikimate Kinase From Erwinia Chrysanthemi within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl803 b:20.8 occ:1.00 O4 B:MPD901 3.1 24.7 1.0 N B:ARG11 3.3 17.6 1.0 NH1 B:ARG139 3.4 11.4 1.0 CA B:GLY79 3.6 14.4 1.0 C4 B:MPD901 3.7 28.7 1.0 CB A:SER114 3.8 18.5 1.0 CA B:ALA10 3.8 14.5 1.0 CG B:ARG11 4.0 22.4 1.0 CB B:ALA10 4.0 13.5 1.0 C B:ALA10 4.1 16.5 1.0 CB B:ARG11 4.1 21.9 1.0 OG A:SER114 4.2 21.0 1.0 CA B:ARG11 4.3 18.8 1.0 CZ B:ARG139 4.3 12.6 1.0 N B:GLY79 4.4 15.5 1.0 C1 B:MPD901 4.4 32.3 1.0 NH2 B:ARG139 4.4 13.3 1.0 C5 B:MPD901 4.4 25.9 1.0 C B:GLY79 4.6 14.3 1.0 O B:ARG11 4.8 19.6 1.0 O B:HOH2019 4.8 18.9 1.0 C3 B:MPD901 4.9 29.6 1.0 OH B:TYR143 4.9 12.8 1.0 O2 B:MPD901 5.0 30.8 1.0 CA A:SER114 5.0 14.9 1.0

T.Krell, J.Maclean, D.J.Boam, A.Cooper, M.Resmini, K.Brocklehurst, S.M.Kelly, N.C.Price, A.J.Lapthorn, J.R.Coggins. Biochemical and X-Ray Crystallographic Studies on Shikimate Kinase: the Important Structural Role of the P-Loop Lysine Protein Sci. V. 10 1137 2001.
ISSN: ISSN 0961-8368
PubMed: 11369852
DOI: 10.1110/PS.52501