Chlorine in PDB 2vjo: Formyl-Coa Transferase Mutant Variant Q17A with Aspartyl-Coa Thioester Intermediates and Oxalate

All present enzymatic activity of Formyl-Coa Transferase Mutant Variant Q17A with Aspartyl-Coa Thioester Intermediates and Oxalate:
2.8.3.16;

The structure of Formyl-Coa Transferase Mutant Variant Q17A with Aspartyl-Coa Thioester Intermediates and Oxalate, PDB code: 2vjo was solved by C.L.Berthold, C.G.Toyota, N.G.J.Richards, Y.Lindqvist, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.20
Space group	I 4
Cell size a, b, c (Å), α, β, γ (°)	153.593, 153.593, 98.055, 90.00, 90.00, 90.00
R / Rfree (%)	20.6 / 24.8

The binding sites of Chlorine atom in the Formyl-Coa Transferase Mutant Variant Q17A with Aspartyl-Coa Thioester Intermediates and Oxalate (pdb code 2vjo). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Formyl-Coa Transferase Mutant Variant Q17A with Aspartyl-Coa Thioester Intermediates and Oxalate, PDB code: 2vjo:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Formyl-Coa Transferase Mutant Variant Q17A with Aspartyl-Coa Thioester Intermediates and Oxalate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Formyl-Coa Transferase Mutant Variant Q17A with Aspartyl-Coa Thioester Intermediates and Oxalate within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1429 b:23.9 occ:1.00 OG A:SER170 2.9 20.3 1.0 O B:HOH2096 3.2 14.1 1.0 CB A:ALA166 3.4 20.0 1.0 N A:SER170 3.4 19.9 1.0 O A:HOH2063 3.4 26.7 1.0 CB A:SER170 3.5 19.6 1.0 CZ A:PHE63 3.5 19.9 1.0 CB A:ALA17 3.5 23.1 1.0 CB A:ASP169 3.8 21.1 1.0 CE2 A:PHE63 3.8 19.0 1.0 CG2 B:ILE210 3.9 20.2 1.0 CA A:SER170 3.9 19.7 1.0 C A:ASP169 4.3 20.3 1.0 CA A:ASP169 4.5 20.7 1.0 O A:HOH2031 4.7 39.6 1.0 CE1 A:PHE63 4.7 20.6 1.0 OE2 A:GLU140 4.7 20.9 1.0 CA A:ALA17 4.8 23.3 1.0 CA A:ALA166 4.9 19.9 1.0 C A:ALA17 4.9 22.6 1.0 O A:ALA17 5.0 22.9 1.0

Chlorine binding site 2 out of 2 in the Formyl-Coa Transferase Mutant Variant Q17A with Aspartyl-Coa Thioester Intermediates and Oxalate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Formyl-Coa Transferase Mutant Variant Q17A with Aspartyl-Coa Thioester Intermediates and Oxalate within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1429 b:21.8 occ:1.00 OG B:SER170 2.9 17.5 1.0 O B:HOH2073 3.0 20.1 1.0 CB B:ALA166 3.2 16.5 1.0 N B:SER170 3.2 18.0 1.0 CB B:SER170 3.4 17.4 1.0 O A:HOH2088 3.4 10.7 1.0 CB B:ASP169 3.7 20.1 1.0 CZ B:PHE63 3.7 16.2 1.0 CB B:ALA17 3.7 18.7 1.0 CE2 B:PHE63 3.8 16.4 1.0 CA B:SER170 3.8 17.6 1.0 CG2 A:ILE210 4.1 17.2 1.0 C B:ASP169 4.2 18.8 1.0 CA B:ASP169 4.4 19.7 1.0 O A:HOH2247 4.5 27.3 1.0 OE1 B:GLU140 4.6 15.3 1.0 CA B:ALA166 4.6 16.2 1.0 CA B:ALA17 4.9 18.9 1.0 C B:ALA17 4.9 18.5 1.0 CE1 B:PHE63 4.9 17.8 1.0

C.L.Berthold, C.G.Toyota, N.G.J.Richards, Y.Lindqvist. Reinvestigation of the Catalytic Mechanism of Formyl-Coa Transferase, A Class III Coa-Transferase. J.Biol.Chem. V. 283 6519 2008.
ISSN: ISSN 0021-9258
PubMed: 18162462
DOI: 10.1074/JBC.M709353200