Magnesium in PDB 2pp1: Crystal Structure of L-Talarate/Galactarate Dehydratase From Salmonella Typhimurium LT2 Liganded with Mg and L-Lyxarohydroxamate

The structure of Crystal Structure of L-Talarate/Galactarate Dehydratase From Salmonella Typhimurium LT2 Liganded with Mg and L-Lyxarohydroxamate, PDB code: 2pp1 was solved by A.A.Fedorov, E.V.Fedorov, W.S.Yew, J.A.Gerlt, S.C.Almo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.87 / 2.20
Space group	P 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	123.187, 173.826, 173.792, 90.00, 90.00, 90.00
R / Rfree (%)	22.3 / 23.7

The binding sites of Magnesium atom in the Crystal Structure of L-Talarate/Galactarate Dehydratase From Salmonella Typhimurium LT2 Liganded with Mg and L-Lyxarohydroxamate (pdb code 2pp1). 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 L-Talarate/Galactarate Dehydratase From Salmonella Typhimurium LT2 Liganded with Mg and L-Lyxarohydroxamate, PDB code: 2pp1:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of L-Talarate/Galactarate Dehydratase From Salmonella Typhimurium LT2 Liganded with Mg and L-Lyxarohydroxamate


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 L-Talarate/Galactarate Dehydratase From Salmonella Typhimurium LT2 Liganded with Mg and L-Lyxarohydroxamate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg399 b:40.9 occ:1.00 O A:HOH944 2.0 36.1 1.0 OE1 A:GLU278 2.2 42.5 1.0 OD2 A:ASP226 2.3 30.6 1.0 ON A:LLH801 2.4 33.5 1.0 OE2 A:GLU252 2.4 23.8 1.0 O1 A:LLH801 2.5 33.6 1.0 N A:LLH801 3.1 36.8 1.0 C1 A:LLH801 3.2 32.2 1.0 CD A:GLU252 3.2 26.6 1.0 CG A:ASP226 3.3 31.0 1.0 CD A:GLU278 3.4 40.3 1.0 NZ A:LYS195 3.6 25.4 1.0 OD1 A:ASP226 3.6 31.1 1.0 O A:HOH827 3.8 21.5 1.0 OE1 A:GLU252 3.9 26.7 1.0 NZ A:LYS197 3.9 29.7 1.0 OE2 A:GLU278 4.0 42.1 1.0 CG A:GLU252 4.0 24.1 1.0 OD1 A:ASN228 4.0 28.5 1.0 OE1 A:GLU253 4.1 34.4 1.0 CD2 A:HIS328 4.2 22.1 1.0 O A:HOH834 4.4 29.4 1.0 CG A:GLU278 4.5 37.5 1.0 CB A:ASP226 4.6 27.9 1.0 NE2 A:HIS328 4.7 21.1 1.0 C2 A:LLH801 4.7 33.0 1.0 CG A:ASN228 4.7 25.6 1.0 CE A:LYS195 4.8 26.7 1.0 OE2 A:GLU348 4.9 25.3 1.0 CD A:GLU253 4.9 31.6 1.0 ND2 A:ASN228 4.9 23.9 1.0 CB A:GLU278 4.9 31.1 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of L-Talarate/Galactarate Dehydratase From Salmonella Typhimurium LT2 Liganded with Mg and L-Lyxarohydroxamate


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 L-Talarate/Galactarate Dehydratase From Salmonella Typhimurium LT2 Liganded with Mg and L-Lyxarohydroxamate within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg444 b:39.8 occ:1.00 O B:HOH939 2.0 34.9 1.0 OE1 B:GLU278 2.2 42.2 1.0 OD2 B:ASP226 2.3 31.5 1.0 ON B:LLH802 2.3 34.2 1.0 OE2 B:GLU252 2.4 22.6 1.0 O1 B:LLH802 2.6 36.0 1.0 N B:LLH802 3.2 38.1 1.0 C1 B:LLH802 3.2 33.5 1.0 CD B:GLU252 3.2 26.4 1.0 CG B:ASP226 3.3 31.3 1.0 CD B:GLU278 3.4 39.9 1.0 NZ B:LYS195 3.6 26.9 1.0 OD1 B:ASP226 3.6 33.0 1.0 O B:HOH828 3.8 20.3 1.0 OE1 B:GLU252 3.9 25.2 1.0 NZ B:LYS197 3.9 27.9 1.0 OE2 B:GLU278 4.0 40.8 1.0 CG B:GLU252 4.0 24.5 1.0 OD1 B:ASN228 4.0 26.7 1.0 OE1 B:GLU253 4.1 32.4 1.0 CD2 B:HIS328 4.2 22.7 1.0 O B:HOH830 4.3 33.2 1.0 CG B:GLU278 4.5 36.5 1.0 CB B:ASP226 4.6 27.4 1.0 NE2 B:HIS328 4.7 23.9 1.0 C2 B:LLH802 4.7 33.4 1.0 CG B:ASN228 4.8 26.9 1.0 CE B:LYS195 4.8 29.3 1.0 OE2 B:GLU348 4.9 24.2 1.0 CD B:GLU253 4.9 30.6 1.0 CB B:GLU278 4.9 30.4 1.0 ND2 B:ASN228 4.9 26.3 1.0

W.S.Yew, A.A.Fedorov, E.V.Fedorov, S.C.Almo, J.A.Gerlt. Evolution of Enzymatic Activities in the Enolase Superfamily: L-Talarate/Galactarate Dehydratase From Salmonella Typhimurium LT2. Biochemistry V. 46 9564 2007.
ISSN: ISSN 0006-2960
PubMed: 17649980
DOI: 10.1021/BI7008882