Cobalt in PDB 1of8: Double Complex of the Tyrosine Sensitive Dahp Synthase From S. Cerevisiae with CO2+, Pep and the E4P Analogoue G3P

All present enzymatic activity of Double Complex of the Tyrosine Sensitive Dahp Synthase From S. Cerevisiae with CO2+, Pep and the E4P Analogoue G3P:
4.1.2.15;

The structure of Double Complex of the Tyrosine Sensitive Dahp Synthase From S. Cerevisiae with CO2+, Pep and the E4P Analogoue G3P, PDB code: 1of8 was solved by V.Koenig, A.Pfeil, G.Heinrich, G.H.Braus, T.R.Schneider, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.00 / 1.50
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	196.462, 50.788, 64.700, 90.00, 106.39, 90.00
R / Rfree (%)	12.5 / 16.7

The binding sites of Cobalt atom in the Double Complex of the Tyrosine Sensitive Dahp Synthase From S. Cerevisiae with CO2+, Pep and the E4P Analogoue G3P (pdb code 1of8). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Double Complex of the Tyrosine Sensitive Dahp Synthase From S. Cerevisiae with CO2+, Pep and the E4P Analogoue G3P, PDB code: 1of8:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the Double Complex of the Tyrosine Sensitive Dahp Synthase From S. Cerevisiae with CO2+, Pep and the E4P Analogoue G3P


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Double Complex of the Tyrosine Sensitive Dahp Synthase From S. Cerevisiae with CO2+, Pep and the E4P Analogoue G3P within 5.0Å range: probe atom residue distance (Å) B Occ A:Co1369 b:18.2 occ:1.00 OE2 A:GLU316 1.9 13.8 1.0 O A:HOH2383 2.1 30.8 1.0 NE2 A:HIS282 2.2 13.9 1.0 OD1 A:ASP342 2.3 18.0 1.0 SG A:CYS76 2.5 17.7 1.0 CD A:GLU316 2.8 12.6 1.0 OE1 A:GLU316 3.1 15.6 1.0 CE1 A:HIS282 3.2 13.6 1.0 CD2 A:HIS282 3.2 12.6 1.0 CG A:ASP342 3.2 20.1 1.0 O1 A:PEP1370 3.5 18.1 1.0 CB A:ASP342 3.5 16.3 1.0 CB A:CYS76 3.5 14.6 1.0 NZ A:LYS112 3.9 13.0 1.0 C1 A:PEP1370 4.0 17.1 1.0 O A:HOH2340 4.1 17.8 1.0 CA A:CYS76 4.1 12.8 1.0 CG A:GLU316 4.2 13.7 1.0 NH2 A:ARG107 4.2 13.4 1.0 ND1 A:HIS282 4.3 12.9 1.0 OD2 A:ASP342 4.3 22.3 1.0 CG A:HIS282 4.3 11.6 1.0 C2 A:PEP1370 4.3 15.7 1.0 O2 A:G3P1371 4.6 28.4 1.0 C3 A:PEP1370 4.7 15.9 1.0 CE A:LYS112 4.7 14.2 1.0 O2' A:PEP1370 4.7 18.6 1.0 O A:CYS76 4.8 13.6 1.0 CA A:ASP342 4.8 17.0 1.0 C1 A:G3P1371 4.8 27.9 1.0 C A:CYS76 4.8 13.1 1.0 N A:ASP342 4.9 16.9 1.0 C2 A:G3P1371 5.0 28.2 1.0 CZ A:ARG107 5.0 12.1 1.0

Cobalt binding site 2 out of 2 in the Double Complex of the Tyrosine Sensitive Dahp Synthase From S. Cerevisiae with CO2+, Pep and the E4P Analogoue G3P


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Double Complex of the Tyrosine Sensitive Dahp Synthase From S. Cerevisiae with CO2+, Pep and the E4P Analogoue G3P within 5.0Å range: probe atom residue distance (Å) B Occ B:Co1372 b:17.4 occ:1.00 O B:HOH2393 1.9 30.1 1.0 OE2 B:GLU316 2.0 14.9 1.0 OD2 B:ASP342 2.2 19.3 1.0 NE2 B:HIS282 2.3 13.0 1.0 SG B:CYS76 2.5 17.9 1.0 CD B:GLU316 2.9 14.7 1.0 CG B:ASP342 3.1 18.0 1.0 OE1 B:GLU316 3.1 15.0 1.0 CE1 B:HIS282 3.2 13.7 1.0 CD2 B:HIS282 3.3 13.8 1.0 O1 B:PEP1373 3.5 22.0 1.0 CB B:ASP342 3.5 17.0 1.0 CB B:CYS76 3.6 15.1 1.0 NZ B:LYS112 3.8 13.3 1.0 C1 B:PEP1373 3.9 16.6 1.0 OD1 B:ASP342 4.1 19.7 1.0 O B:HOH2341 4.2 18.7 1.0 CA B:CYS76 4.2 14.6 1.0 NH2 B:ARG107 4.2 12.8 1.0 CG B:GLU316 4.2 14.5 1.0 C2 B:PEP1373 4.2 16.1 1.0 ND1 B:HIS282 4.3 12.4 1.0 CG B:HIS282 4.4 13.0 1.0 O2 B:G3P1374 4.5 24.4 1.0 C3 B:PEP1373 4.5 17.1 1.0 O2' B:PEP1373 4.6 19.5 1.0 CE B:LYS112 4.7 13.5 1.0 C1 B:G3P1374 4.7 24.1 1.0 CA B:ASP342 4.8 16.5 1.0 O B:CYS76 4.8 13.1 1.0 C2 B:G3P1374 4.9 23.6 1.0 N B:ASP342 4.9 16.9 1.0 C B:CYS76 4.9 14.2 1.0 O2 B:PEP1373 4.9 13.8 1.0 CZ B:ARG107 5.0 12.8 1.0

V.Koenig, A.Pfeil, G.H.Braus, T.R.Schneider. Substrate and Metal Complexes of 3-Deoxy-D-Arabino-Heptulosonate-7-Phosphate Synthase From Saccharomyces Cerevisiae Provide New Insights Into the Catalytic Mechanism J.Mol.Biol. V. 337 675 2004.
ISSN: ISSN 0022-2836
PubMed: 15019786
DOI: 10.1016/J.JMB.2004.01.055