Chlorine in PDB 3tpz: 2.1 Angstrom Crystal Structure of the L114P Mutant of E. Coli Ksga

All present enzymatic activity of 2.1 Angstrom Crystal Structure of the L114P Mutant of E. Coli Ksga:
2.1.1.182;

The structure of 2.1 Angstrom Crystal Structure of the L114P Mutant of E. Coli Ksga, PDB code: 3tpz was solved by J.N.Scarsdale, F.N.Musayev, J.P.Rife, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.00 / 2.10
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	239.007, 38.534, 64.752, 90.00, 96.34, 90.00
R / Rfree (%)	21.1 / 27.6

The binding sites of Chlorine atom in the 2.1 Angstrom Crystal Structure of the L114P Mutant of E. Coli Ksga (pdb code 3tpz). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the 2.1 Angstrom Crystal Structure of the L114P Mutant of E. Coli Ksga, PDB code: 3tpz:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the 2.1 Angstrom Crystal Structure of the L114P Mutant of E. Coli Ksga


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of 2.1 Angstrom Crystal Structure of the L114P Mutant of E. Coli Ksga within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl274 b:65.5 occ:1.00 O A:HOH297 2.9 59.5 1.0 N A:ARG159 3.2 46.4 1.0 CA A:GLY158 3.6 44.3 1.0 NH2 A:ARG147 3.7 54.5 1.0 C A:GLY158 3.8 43.6 1.0 N A:LEU160 4.0 47.3 1.0 CB A:ARG159 4.1 50.3 1.0 CA A:ARG159 4.1 47.7 1.0 NE A:ARG147 4.2 59.9 1.0 CZ A:ARG147 4.4 57.4 1.0 C A:ARG159 4.6 47.7 1.0 N A:GLY158 4.7 44.1 1.0 CB A:LEU160 4.8 44.9 1.0 O A:GLY158 4.8 43.4 1.0 NH1 A:ARG221 4.9 63.8 1.0

Chlorine binding site 2 out of 2 in the 2.1 Angstrom Crystal Structure of the L114P Mutant of E. Coli Ksga


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of 2.1 Angstrom Crystal Structure of the L114P Mutant of E. Coli Ksga within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl275 b:54.4 occ:1.00 O A:HOH280 2.9 33.9 1.0 NH2 A:ARG74 3.6 36.2 1.0 NH1 A:ARG74 3.9 37.2 1.0 CZ A:ARG74 4.2 40.9 1.0 O A:LEU48 4.3 27.2 1.0 OE2 A:GLU53 4.9 32.4 1.0

H.C.O'farrell, F.N.Musayev, J.N.Scarsdale, J.P.Rife. Control of Substrate Specificity By A Single Active Site Residue of the Ksga Methyltransferase. Biochemistry V. 51 466 2012.
ISSN: ISSN 0006-2960
PubMed: 22142337
DOI: 10.1021/BI201539J