Chlorine in PDB 4orf: Camp-Binding Acyltransferase From Mycobacterium Smegmatis, Mutant R95K

The structure of Camp-Binding Acyltransferase From Mycobacterium Smegmatis, Mutant R95K, PDB code: 4orf was solved by M.Podobnik, K.Rebolj, S.S.Visweswariah, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	38.295, 82.847, 104.370, 90.00, 90.00, 90.00
R / Rfree (%)	22 / 27.6

The binding sites of Chlorine atom in the Camp-Binding Acyltransferase From Mycobacterium Smegmatis, Mutant R95K (pdb code 4orf). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Camp-Binding Acyltransferase From Mycobacterium Smegmatis, Mutant R95K, PDB code: 4orf:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Camp-Binding Acyltransferase From Mycobacterium Smegmatis, Mutant R95K


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Camp-Binding Acyltransferase From Mycobacterium Smegmatis, Mutant R95K within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:33.0 occ:1.00 O A:HOH575 3.0 27.5 1.0 N A:ARG186 3.1 32.5 1.0 CD A:ARG186 3.7 36.9 1.0 CB A:ARG186 3.7 33.2 1.0 CB A:ASP92 3.9 32.2 1.0 CG A:ARG186 3.9 38.6 1.0 CA A:ARG186 3.9 33.7 1.0 C A:VAL185 4.0 37.5 1.0 O A:SER184 4.0 41.7 1.0 CA A:VAL185 4.0 35.5 1.0 O A:HOH517 4.0 53.3 1.0 NH1 A:ARG112 4.1 32.4 1.0 OD2 A:ASP92 4.4 36.8 1.0 O A:ARG186 4.6 29.4 1.0 CG A:ASP92 4.6 33.1 1.0 NH1 A:ARG186 4.6 46.0 1.0 CG1 A:VAL185 4.6 34.0 1.0 O A:LEU90 4.7 36.2 1.0 C A:ARG186 4.8 31.6 1.0 NE A:ARG186 4.9 43.9 1.0 CB A:VAL185 4.9 37.3 1.0 C A:SER184 4.9 40.9 1.0 N A:VAL185 5.0 39.3 1.0

Chlorine binding site 2 out of 3 in the Camp-Binding Acyltransferase From Mycobacterium Smegmatis, Mutant R95K


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Camp-Binding Acyltransferase From Mycobacterium Smegmatis, Mutant R95K within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl402 b:80.7 occ:1.00 O A:GLU79 3.3 65.1 1.0 CD2 A:LEU82 3.5 67.8 1.0 CG2 A:ILE78 3.6 61.0 1.0 CB A:ILE78 3.9 65.7 1.0 CD1 A:LEU82 4.0 59.6 1.0 CG A:LEU82 4.0 62.4 1.0 CB A:LEU82 4.2 57.3 1.0 C A:GLU79 4.3 72.3 1.0 N A:GLU79 4.6 68.3 1.0 O A:PRO80 4.7 76.1 1.0 CA A:ILE78 4.8 68.6 1.0 CA A:GLU79 4.8 72.9 1.0 C A:ILE78 4.9 67.3 1.0 CG1 A:ILE78 4.9 65.2 1.0 CB A:GLU79 5.0 80.6 1.0

Chlorine binding site 3 out of 3 in the Camp-Binding Acyltransferase From Mycobacterium Smegmatis, Mutant R95K


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Camp-Binding Acyltransferase From Mycobacterium Smegmatis, Mutant R95K within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl403 b:67.2 occ:1.00 O A:HOH585 2.6 33.1 1.0 NH2 A:ARG190 3.2 33.5 1.0 NE A:ARG190 3.8 30.8 1.0 CZ A:ARG190 4.0 32.0 1.0

M.Podobnik, N.Siddiqui, K.Rebolj, S.Nambi, F.Merzel, S.S.Visweswariah. Allostery and Conformational Dynamics in Camp-Binding Acyltransferases. J.Biol.Chem. V. 289 16588 2014.
ISSN: ISSN 0021-9258
PubMed: 24748621
DOI: 10.1074/JBC.M114.560086