Magnesium in PDB 2c42: Crystal Structure of Pyruvate-Ferredoxin Oxidoreductase From Desulfovibrio Africanus

All present enzymatic activity of Crystal Structure of Pyruvate-Ferredoxin Oxidoreductase From Desulfovibrio Africanus:
1.2.7.1;

The structure of Crystal Structure of Pyruvate-Ferredoxin Oxidoreductase From Desulfovibrio Africanus, PDB code: 2c42 was solved by C.Cavazza, C.Contreras-Martel, L.Pieulle, E.Chabriere, E.C.Hatchikian, J.C.Fontecilla-Camps, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	51.15 / 1.78
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	86.304, 145.981, 211.607, 90.00, 90.00, 90.00
R / Rfree (%)	19.5 / 21.9

The structure of Crystal Structure of Pyruvate-Ferredoxin Oxidoreductase From Desulfovibrio Africanus also contains other interesting chemical elements:

Iron	(Fe)	24 atoms
Calcium	(Ca)	2 atoms

The binding sites of Magnesium atom in the Crystal Structure of Pyruvate-Ferredoxin Oxidoreductase From Desulfovibrio Africanus (pdb code 2c42). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Pyruvate-Ferredoxin Oxidoreductase From Desulfovibrio Africanus, PDB code: 2c42:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Pyruvate-Ferredoxin Oxidoreductase From Desulfovibrio Africanus


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Pyruvate-Ferredoxin Oxidoreductase From Desulfovibrio Africanus within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg3238 b:12.4 occ:1.00 OD1 A:ASP963 2.0 15.7 1.0 O1B A:TPP3236 2.1 12.7 1.0 O A:VAL993 2.1 16.6 1.0 O2A A:TPP3236 2.1 13.1 1.0 O A:HOH2438 2.2 18.1 1.0 OG1 A:THR991 2.3 16.3 1.0 CG A:ASP963 3.0 11.2 1.0 PB A:TPP3236 3.3 17.2 1.0 PA A:TPP3236 3.3 15.3 1.0 C A:VAL993 3.3 18.5 1.0 O3A A:TPP3236 3.4 13.6 1.0 OD2 A:ASP963 3.5 16.3 1.0 CB A:THR991 3.6 19.1 1.0 N A:ASP963 3.8 14.1 1.0 N A:THR991 3.9 17.6 1.0 O2B A:TPP3236 3.9 15.9 1.0 N A:SER995 3.9 13.6 1.0 N A:VAL993 4.0 18.3 1.0 O7 A:TPP3236 4.0 18.1 1.0 OG A:SER995 4.0 14.7 1.0 CG2 A:THR991 4.1 18.4 1.0 N A:TYR994 4.2 17.3 1.0 CA A:THR991 4.2 16.9 1.0 CA A:TYR994 4.2 15.4 1.0 CB A:ASP963 4.2 13.9 1.0 N A:GLY964 4.3 12.1 1.0 CA A:VAL993 4.3 19.8 1.0 O A:MET989 4.4 20.3 1.0 C A:THR991 4.5 15.9 1.0 O1A A:TPP3236 4.5 13.2 1.0 CA A:ASP963 4.5 12.5 1.0 O3B A:TPP3236 4.5 20.2 1.0 CA A:GLY962 4.5 14.0 1.0 N A:GLU992 4.5 17.0 1.0 C A:TYR994 4.6 14.7 1.0 CB A:SER995 4.6 12.6 1.0 C A:GLY962 4.6 14.6 1.0 CG1 A:VAL993 4.8 21.5 1.0 CA A:SER995 4.9 13.5 1.0 C A:ASP963 4.9 16.0 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Pyruvate-Ferredoxin Oxidoreductase From Desulfovibrio Africanus


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Pyruvate-Ferredoxin Oxidoreductase From Desulfovibrio Africanus within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg3238 b:9.1 occ:1.00 O1B B:TPP3236 2.1 13.2 1.0 OD1 B:ASP963 2.1 11.8 1.0 OG1 B:THR991 2.2 12.5 1.0 O2A B:TPP3236 2.2 12.3 1.0 O B:VAL993 2.2 14.7 1.0 O B:HOH2549 2.2 12.7 1.0 CG B:ASP963 3.1 12.9 1.0 PB B:TPP3236 3.3 13.5 1.0 PA B:TPP3236 3.3 12.6 1.0 C B:VAL993 3.4 16.2 1.0 O3A B:TPP3236 3.4 12.1 1.0 CB B:THR991 3.5 15.4 1.0 OD2 B:ASP963 3.6 10.5 1.0 N B:ASP963 3.8 8.7 1.0 N B:THR991 3.8 13.8 1.0 O2B B:TPP3236 3.9 12.3 1.0 N B:SER995 3.9 11.3 1.0 OG B:SER995 3.9 12.6 1.0 CG2 B:THR991 4.0 10.9 1.0 O7 B:TPP3236 4.1 13.7 1.0 N B:VAL993 4.1 17.0 1.0 CA B:THR991 4.1 12.1 1.0 CA B:TYR994 4.2 13.7 1.0 N B:TYR994 4.2 15.7 1.0 N B:GLY964 4.3 12.4 1.0 CB B:ASP963 4.3 12.1 1.0 CA B:VAL993 4.4 18.0 1.0 O B:MET989 4.4 15.2 1.0 C B:THR991 4.5 12.6 1.0 O3B B:TPP3236 4.5 13.0 1.0 O1A B:TPP3236 4.5 11.7 1.0 N B:GLU992 4.5 12.0 1.0 CB B:SER995 4.5 11.8 1.0 C B:TYR994 4.5 12.2 1.0 CA B:ASP963 4.5 11.0 1.0 CA B:GLY962 4.6 10.8 1.0 C B:GLY962 4.6 10.3 1.0 CA B:SER995 4.8 9.4 1.0 CG2 B:VAL993 4.9 17.6 1.0 C B:ASP963 4.9 10.4 1.0

C.Cavazza, C.Contreras-Martel, L.Pieulle, E.Chabriere, E.C.Hatchikian, J.C.Fontecilla-Camps. Flexibility of Thiamine Diphosphate Revealed By Kinetic Crystallographic Studies of the Reaction of Pyruvate-Ferredoxin Oxidoreductase with Pyruvate. Structure V. 14 217 2006.
ISSN: ISSN 0969-2126
PubMed: 16472741
DOI: 10.1016/J.STR.2005.10.013