Magnesium in PDB 1m1b: Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Sulfopyruvate

All present enzymatic activity of Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Sulfopyruvate:
5.4.2.9;

The structure of Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Sulfopyruvate, PDB code: 1m1b was solved by S.Liu, Z.Lu, Y.Jia, D.Dunaway-Mariano, O.Herzberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.50 / 2.25
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	90.024, 130.441, 90.475, 90.00, 90.00, 90.00
R / Rfree (%)	17.9 / 26.8

The binding sites of Magnesium atom in the Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Sulfopyruvate (pdb code 1m1b). 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 Phosphoenolpyruvate Mutase Complexed with Sulfopyruvate, PDB code: 1m1b:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Sulfopyruvate


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 Phosphoenolpyruvate Mutase Complexed with Sulfopyruvate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg998 b:24.8 occ:1.00 OD2 A:ASP85 2.1 32.7 1.0 O2' A:SPV996 2.2 32.7 1.0 O2 A:SPV996 2.3 40.9 1.0 O A:HOH1107 2.3 44.0 1.0 O A:HOH1108 2.5 24.4 1.0 O A:HOH1109 2.5 22.2 1.0 C2 A:SPV996 2.6 40.9 1.0 C1 A:SPV996 2.7 39.9 1.0 CG A:ASP85 3.2 30.7 1.0 O1S A:SPV996 3.4 44.3 1.0 OD1 A:ASP85 3.6 31.9 1.0 C3 A:SPV996 3.7 44.0 1.0 NH2 A:ARG159 3.7 42.0 1.0 NH1 A:ARG159 3.7 44.3 1.0 NZ A:LYS120 3.8 36.0 1.0 O1 A:SPV996 4.0 43.0 1.0 OD2 A:ASP58 4.0 34.5 1.0 S A:SPV996 4.1 46.1 1.0 N A:GLY47 4.1 26.2 1.0 CZ A:ARG159 4.2 41.6 1.0 CA A:GLY47 4.2 25.4 1.0 N A:LEU48 4.3 25.7 1.0 OD1 A:ASP87 4.3 30.2 1.0 CB A:ASP85 4.4 30.1 1.0 O2S A:SPV996 4.4 43.7 1.0 O A:HOH1063 4.5 28.3 1.0 OD1 A:ASP58 4.5 33.7 1.0 CG A:ASP58 4.7 30.5 1.0 C A:GLY47 4.7 25.5 1.0 ND2 A:ASN122 4.8 30.4 1.0 OE1 A:GLU114 4.9 35.6 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Sulfopyruvate


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 Phosphoenolpyruvate Mutase Complexed with Sulfopyruvate within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg999 b:28.6 occ:1.00 O B:HOH1111 1.9 41.2 1.0 O2' B:SPV997 2.0 44.4 1.0 O B:HOH1112 2.1 32.2 1.0 OD2 B:ASP85 2.3 35.3 1.0 O B:HOH1110 2.4 24.9 1.0 O2 B:SPV997 2.5 46.4 1.0 C1 B:SPV997 2.7 46.0 1.0 C2 B:SPV997 2.8 45.7 1.0 CG B:ASP85 3.2 32.9 1.0 OD1 B:ASP85 3.5 32.3 1.0 O1S B:SPV997 3.7 45.5 1.0 NH1 B:ARG159 3.8 21.6 1.0 O1 B:SPV997 3.9 45.8 1.0 C3 B:SPV997 4.0 45.5 1.0 OD1 B:ASP87 4.1 25.1 1.0 OD2 B:ASP58 4.1 29.6 1.0 NH2 B:ARG159 4.1 22.1 1.0 N B:LEU48 4.3 25.4 1.0 N B:GLY47 4.3 24.1 1.0 OD1 B:ASP58 4.4 30.8 1.0 CZ B:ARG159 4.4 26.3 1.0 S B:SPV997 4.4 46.0 1.0 CB B:ASP85 4.5 32.2 1.0 CA B:GLY47 4.5 25.4 1.0 NZ B:LYS120 4.5 38.3 1.0 CG B:ASP58 4.7 29.1 1.0 CE B:LYS120 4.7 35.1 1.0 O2S B:SPV997 4.8 46.0 1.0 OE1 B:GLU114 4.8 21.1 1.0 C B:GLY47 4.9 27.0 1.0

S.Liu, Z.Lu, Y.Jia, D.Dunaway-Mariano, O.Herzberg. Dissociative Phosphoryl Transfer in Pep Mutase Catalysis: Structure of the Enzyme/Sulfopyruvate Complex and Kinetic Properties of Mutants. Biochemistry V. 41 10270 2002.
ISSN: ISSN 0006-2960
PubMed: 12162742
DOI: 10.1021/BI026024V