Chlorine in PDB 3rv4: Crystal Structure of E.Coli Biotin Carboxylase R16E Mutant in Complex with Mg-Adp and Bicarbonate

All present enzymatic activity of Crystal Structure of E.Coli Biotin Carboxylase R16E Mutant in Complex with Mg-Adp and Bicarbonate:
6.3.4.14; 6.4.1.2;

The structure of Crystal Structure of E.Coli Biotin Carboxylase R16E Mutant in Complex with Mg-Adp and Bicarbonate, PDB code: 3rv4 was solved by C.Y.Chou, L.Tong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.98
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	119.404, 51.171, 84.156, 90.00, 119.75, 90.00
R / Rfree (%)	17.9 / 21.9

The structure of Crystal Structure of E.Coli Biotin Carboxylase R16E Mutant in Complex with Mg-Adp and Bicarbonate also contains other interesting chemical elements:

Magnesium	(Mg)	1 atom
Caesium	(Cs)	1 atom
Sodium	(Na)	2 atoms

The binding sites of Chlorine atom in the Crystal Structure of E.Coli Biotin Carboxylase R16E Mutant in Complex with Mg-Adp and Bicarbonate (pdb code 3rv4). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of E.Coli Biotin Carboxylase R16E Mutant in Complex with Mg-Adp and Bicarbonate, PDB code: 3rv4:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of E.Coli Biotin Carboxylase R16E Mutant in Complex with Mg-Adp and Bicarbonate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of E.Coli Biotin Carboxylase R16E Mutant in Complex with Mg-Adp and Bicarbonate within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1010 b:10.2 occ:1.00 O A:ASN429 3.3 14.7 1.0 O A:GLY433 3.4 22.2 1.0 CG2 A:THR435 3.8 15.3 1.0 C A:ASN429 4.1 14.2 1.0 CB A:HIS432 4.2 23.6 1.0 CA A:ASN429 4.2 14.3 1.0 C A:GLY433 4.3 21.9 1.0 CB A:ASN429 4.4 13.8 1.0 N A:GLY433 4.5 23.1 1.0 N A:THR435 4.6 18.2 1.0 OD1 A:ASN429 4.8 12.3 1.0 C A:HIS432 4.8 22.9 1.0 C A:GLY434 4.8 19.6 1.0 CA A:THR435 4.9 16.1 1.0 CB A:THR435 5.0 16.3 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of E.Coli Biotin Carboxylase R16E Mutant in Complex with Mg-Adp and Bicarbonate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of E.Coli Biotin Carboxylase R16E Mutant in Complex with Mg-Adp and Bicarbonate within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl451 b:23.9 occ:1.00 O A:HOH478 2.6 9.3 1.0 N A:ILE293 2.8 11.2 1.0 O A:GLY81 2.9 12.0 1.0 NE2 A:GLN312 3.0 9.3 1.0 CG2 A:ILE293 3.3 10.5 1.0 CB A:ILE293 3.4 11.3 1.0 CE1 A:HIS79 3.5 11.5 1.0 CA A:ILE293 3.7 11.5 1.0 C A:ARG292 3.7 11.4 1.0 CA A:ARG292 3.8 10.9 1.0 C A:GLY81 3.8 12.6 1.0 CB A:ARG292 3.9 11.0 1.0 CD A:GLN312 4.1 12.7 1.0 ND1 A:HIS79 4.2 10.4 1.0 CA A:GLY81 4.2 12.5 1.0 OE1 A:GLN312 4.3 12.0 1.0 N A:GLY81 4.3 13.0 1.0 NE2 A:HIS79 4.4 10.3 1.0 CG A:PRO80 4.5 12.6 1.0 O A:ILE293 4.5 11.4 1.0 C A:ILE293 4.6 12.1 1.0 O A:ILE103 4.6 14.1 1.0 O A:HOH461 4.7 12.4 1.0 CD A:PRO80 4.8 11.7 1.0 N A:TYR82 4.8 12.8 1.0 CG1 A:ILE293 4.9 12.8 1.0 O A:ARG292 4.9 11.2 1.0

C.Y.Chou, L.Tong. Structural and Biochemical Studies on the Regulation of Biotin Carboxylase By Substrate Inhibition and Dimerization. J.Biol.Chem. V. 286 24417 2011.
ISSN: ISSN 0021-9258
PubMed: 21592965
DOI: 10.1074/JBC.M111.220517