Magnesium in PDB 2pp3: Crystal Structure of L-Talarate/Galactarate Dehydratase Mutant K197A Liganded with Mg and L-Glucarate

The structure of Crystal Structure of L-Talarate/Galactarate Dehydratase Mutant K197A Liganded with Mg and L-Glucarate, PDB code: 2pp3 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)	24.94 / 2.20
Space group	P 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	174.234, 174.234, 123.573, 90.00, 90.00, 90.00
R / Rfree (%)	20.4 / 23.1

The binding sites of Magnesium atom in the Crystal Structure of L-Talarate/Galactarate Dehydratase Mutant K197A Liganded with Mg and L-Glucarate (pdb code 2pp3). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of L-Talarate/Galactarate Dehydratase Mutant K197A Liganded with Mg and L-Glucarate, PDB code: 2pp3:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Crystal Structure of L-Talarate/Galactarate Dehydratase Mutant K197A Liganded with Mg and L-Glucarate


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 Mutant K197A Liganded with Mg and L-Glucarate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg901 b:26.7 occ:1.00 OE1 A:GLU278 2.1 24.4 1.0 OD2 A:ASP226 2.2 28.4 1.0 O A:HOH1053 2.2 25.9 1.0 O1B A:LGT501 2.2 23.7 1.0 O2 A:LGT501 2.2 26.3 1.0 OE2 A:GLU252 2.3 25.9 1.0 CD A:GLU278 3.0 27.8 1.0 C1 A:LGT501 3.0 26.6 1.0 C2 A:LGT501 3.1 26.9 1.0 OE2 A:GLU278 3.2 28.3 1.0 CG A:ASP226 3.2 29.3 1.0 CD A:GLU252 3.3 27.1 1.0 OD1 A:ASP226 3.6 31.1 1.0 NZ A:LYS195 3.9 22.9 1.0 OD1 A:ASN228 3.9 30.1 1.0 O A:HOH952 3.9 25.2 1.0 CG A:GLU252 4.0 24.4 1.0 O A:HOH1052 4.2 37.8 1.0 O A:HOH918 4.2 20.8 1.0 O1A A:LGT501 4.2 27.2 1.0 OE1 A:GLU252 4.2 27.7 1.0 CD2 A:HIS328 4.3 19.3 1.0 CG A:GLU278 4.3 25.3 1.0 C3 A:LGT501 4.4 27.3 1.0 OE1 A:GLU253 4.4 32.8 1.0 O3 A:LGT501 4.4 27.7 1.0 CB A:ASP226 4.5 25.1 1.0 CE A:LYS195 4.6 25.4 1.0 CG A:ASN228 4.7 26.6 1.0 NE2 A:HIS328 4.8 20.9 1.0 CB A:GLU278 4.9 23.7 1.0 ND2 A:ASN228 5.0 25.0 1.0 O4 A:LGT501 5.0 31.4 1.0 CG A:GLU253 5.0 28.1 1.0

Magnesium binding site 2 out of 3 in the Crystal Structure of L-Talarate/Galactarate Dehydratase Mutant K197A Liganded with Mg and L-Glucarate


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 Mutant K197A Liganded with Mg and L-Glucarate within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg902 b:41.7 occ:1.00 OD2 B:ASP226 2.1 37.4 1.0 O B:HOH980 2.2 36.9 1.0 O2 B:LGT502 2.3 37.9 1.0 O1B B:LGT502 2.3 39.5 1.0 OE2 B:GLU252 2.3 30.8 1.0 OE1 B:GLU278 2.3 38.1 1.0 C1 B:LGT502 3.1 39.7 1.0 CG B:ASP226 3.1 37.8 1.0 C2 B:LGT502 3.1 39.3 1.0 CD B:GLU252 3.2 30.9 1.0 CD B:GLU278 3.3 36.5 1.0 OE2 B:GLU278 3.5 37.7 1.0 OD1 B:ASP226 3.5 38.0 1.0 NZ B:LYS195 3.7 33.9 1.0 O B:HOH979 4.0 37.3 1.0 CG B:GLU252 4.0 29.9 1.0 OD1 B:ASN228 4.0 38.4 1.0 OE1 B:GLU252 4.1 35.0 1.0 O1A B:LGT502 4.3 38.0 1.0 CB B:ASP226 4.3 34.8 1.0 CD2 B:HIS328 4.4 33.6 1.0 OE1 B:GLU253 4.4 40.6 1.0 O B:HOH904 4.4 26.7 1.0 C3 B:LGT502 4.5 40.7 1.0 CE B:LYS195 4.5 32.1 1.0 O3 B:LGT502 4.6 40.2 1.0 CG B:GLU278 4.6 33.9 1.0 CG B:ASN228 4.7 37.3 1.0 ND2 B:ASN228 4.8 34.4 1.0 NE2 B:HIS328 4.8 34.7 1.0 CB B:GLU252 5.0 27.2 1.0

Magnesium binding site 3 out of 3 in the Crystal Structure of L-Talarate/Galactarate Dehydratase Mutant K197A Liganded with Mg and L-Glucarate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of L-Talarate/Galactarate Dehydratase Mutant K197A Liganded with Mg and L-Glucarate within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg903 b:50.9 occ:1.00 O C:HOH976 2.1 44.2 1.0 OD2 C:ASP226 2.3 45.2 1.0 OE1 C:GLU278 2.3 37.3 1.0 OE2 C:GLU252 2.3 40.9 1.0 O2 C:LGT503 2.3 42.9 1.0 O1B C:LGT503 2.4 43.8 1.0 C1 C:LGT503 3.2 46.6 1.0 CG C:ASP226 3.2 44.0 1.0 CD C:GLU278 3.2 39.6 1.0 C2 C:LGT503 3.2 45.8 1.0 CD C:GLU252 3.3 40.0 1.0 OE2 C:GLU278 3.4 40.8 1.0 NZ C:LYS195 3.6 37.1 1.0 OD1 C:ASP226 3.7 44.0 1.0 O C:HOH972 4.0 45.9 1.0 OE1 C:GLU252 4.1 38.7 1.0 OD1 C:ASN228 4.1 46.5 1.0 O C:HOH958 4.1 37.7 1.0 CG C:GLU252 4.1 38.3 1.0 CB C:ASP226 4.3 41.4 1.0 O1A C:LGT503 4.4 47.9 1.0 O C:HOH910 4.4 26.8 1.0 CD2 C:HIS328 4.5 35.6 1.0 OE1 C:GLU253 4.5 40.0 1.0 C3 C:LGT503 4.5 45.0 1.0 CG C:GLU278 4.6 35.9 1.0 O3 C:LGT503 4.6 45.4 1.0 CE C:LYS195 4.8 39.3 1.0 CG C:ASN228 4.9 43.5 1.0 NE2 C:HIS328 4.9 36.8 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