Manganese in PDB 6v2l: E. Coli Phosphoenolpyruvate Carboxykinase S250A

All present enzymatic activity of E. Coli Phosphoenolpyruvate Carboxykinase S250A:
4.1.1.49;

The structure of E. Coli Phosphoenolpyruvate Carboxykinase S250A, PDB code: 6v2l was solved by A.S.Sokaribo, H.Goldie, D.Sanders, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.50 / 1.70
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	124.910, 94.620, 46.350, 90.00, 96.21, 90.00
R / Rfree (%)	16.7 / 20.8

The binding sites of Manganese atom in the E. Coli Phosphoenolpyruvate Carboxykinase S250A (pdb code 6v2l). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the E. Coli Phosphoenolpyruvate Carboxykinase S250A, PDB code: 6v2l:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the E. Coli Phosphoenolpyruvate Carboxykinase S250A


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of E. Coli Phosphoenolpyruvate Carboxykinase S250A within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn603 b:12.8 occ:1.00 O A:HOH740 2.0 14.0 1.0 O2B A:ATP601 2.0 13.8 1.0 O3G A:ATP601 2.1 13.3 1.0 O A:HOH721 2.1 13.8 1.0 OG1 A:THR255 2.1 11.9 1.0 O A:HOH749 2.1 15.6 1.0 PG A:ATP601 3.2 14.7 1.0 CB A:THR255 3.2 12.9 1.0 PB A:ATP601 3.2 14.7 1.0 O3B A:ATP601 3.5 16.4 1.0 O1G A:ATP601 3.7 15.3 1.0 OD2 A:ASP268 3.7 13.4 1.0 O A:TYR286 3.8 13.5 1.0 O2A A:ATP601 3.9 14.6 1.0 N A:THR255 4.0 13.4 1.0 O A:ASP268 4.1 14.2 1.0 OD1 A:ASP269 4.1 13.4 1.0 NH1 A:ARG333 4.1 14.7 1.0 O3A A:ATP601 4.2 14.8 1.0 O A:HOH928 4.2 14.1 1.0 CA A:THR255 4.2 11.1 1.0 CG2 A:THR255 4.2 13.5 1.0 O1B A:ATP601 4.4 12.3 1.0 O2G A:ATP601 4.4 13.2 1.0 PA A:ATP601 4.4 16.0 1.0 CG A:ASP268 4.6 13.2 1.0 CG A:ASP269 4.7 13.7 1.0 CB A:ASP269 4.7 13.2 1.0 C A:TYR286 4.8 15.1 1.0 O1A A:ATP601 4.8 15.4 1.0 CB A:LYS254 4.9 12.9 1.0 MN A:MN604 5.0 11.9 1.0 CE A:LYS254 5.0 12.6 1.0 C A:ASP268 5.0 14.0 1.0

Manganese binding site 2 out of 2 in the E. Coli Phosphoenolpyruvate Carboxykinase S250A


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of E. Coli Phosphoenolpyruvate Carboxykinase S250A within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn604 b:11.9 occ:1.00 NE2 A:HIS232 2.1 14.5 1.0 NZ A:LYS213 2.1 12.1 1.0 O1G A:ATP601 2.2 15.3 1.0 O A:HOH948 2.2 16.0 1.0 OD1 A:ASP269 2.2 13.4 1.0 O A:HOH928 2.2 14.1 1.0 CG A:ASP269 3.0 13.7 1.0 CD2 A:HIS232 3.0 15.7 1.0 CE A:LYS213 3.1 16.9 1.0 CE1 A:HIS232 3.1 15.1 1.0 OD2 A:ASP269 3.1 16.4 1.0 PG A:ATP601 3.3 14.7 1.0 O2G A:ATP601 3.7 13.2 1.0 O3G A:ATP601 3.8 13.3 1.0 O A:HOH740 4.0 14.0 1.0 NZ A:LYS254 4.1 13.2 1.0 CG A:HIS232 4.2 16.1 1.0 ND1 A:HIS232 4.2 17.0 1.0 CE A:LYS254 4.2 12.6 1.0 O A:HOH1170 4.3 24.1 1.0 CB A:ASP269 4.4 13.2 1.0 CD A:LYS213 4.5 18.1 1.0 O A:HOH1103 4.6 27.8 1.0 O3B A:ATP601 4.6 16.4 1.0 CE2 A:PHE413 4.6 14.4 1.0 O A:ASP269 4.9 13.1 1.0 CZ A:PHE413 4.9 15.2 1.0 MN A:MN603 5.0 12.8 1.0

A.S.Sokaribo, J.H.Cotelesage, B.Novakovski, H.Goldie, D.Sanders. E. Coli Phosphoenolpyruvate Carboxykinase S250A Mutant To Be Published.