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Magnesium in PDB 1mum: Structure of the 2-Methylisocitrate Lyase (Prpb) From Escherichia Coli

Enzymatic activity of Structure of the 2-Methylisocitrate Lyase (Prpb) From Escherichia Coli

All present enzymatic activity of Structure of the 2-Methylisocitrate Lyase (Prpb) From Escherichia Coli:
4.1.3.30;

Protein crystallography data

The structure of Structure of the 2-Methylisocitrate Lyase (Prpb) From Escherichia Coli, PDB code: 1mum was solved by C.Grimm, K.Reuter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.35 / 1.90
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 82.895, 82.895, 166.250, 90.00, 90.00, 120.00
R / Rfree (%) 21.3 / 23.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of the 2-Methylisocitrate Lyase (Prpb) From Escherichia Coli (pdb code 1mum). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of the 2-Methylisocitrate Lyase (Prpb) From Escherichia Coli, PDB code: 1mum:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1mum

Go back to Magnesium Binding Sites List in 1mum
Magnesium binding site 1 out of 2 in the Structure of the 2-Methylisocitrate Lyase (Prpb) From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the 2-Methylisocitrate Lyase (Prpb) From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1001

b:37.0
occ:1.00
O A:HOH1044 2.1 34.8 1.0
O A:HOH1076 2.1 24.9 1.0
O A:HOH1093 2.2 29.5 1.0
O A:HOH1031 2.3 25.0 1.0
OD1 A:ASP87 2.3 28.3 1.0
O A:HOH1006 2.6 24.3 1.0
CG A:ASP87 3.4 25.5 1.0
OD2 A:ASP58 3.5 29.8 1.0
OD1 A:ASP58 3.7 26.3 1.0
OD2 A:ASP87 3.9 25.6 1.0
OD2 A:ASP85 4.0 19.9 1.0
CG A:ASP58 4.0 28.3 1.0
O A:HOH1160 4.1 35.8 1.0
OE1 A:GLU115 4.1 20.0 1.0
OE2 A:GLU115 4.2 23.3 1.0
O A:HOH1186 4.3 42.8 1.0
OD1 A:ASP85 4.5 16.7 1.0
CD A:GLU115 4.5 22.2 1.0
CB A:ASP87 4.7 20.9 1.0
CG A:ASP85 4.7 17.2 1.0
O A:HOH1090 4.7 43.9 1.0
NH1 A:ARG158 4.9 24.7 1.0
CA A:ASP87 5.0 21.2 1.0

Magnesium binding site 2 out of 2 in 1mum

Go back to Magnesium Binding Sites List in 1mum
Magnesium binding site 2 out of 2 in the Structure of the 2-Methylisocitrate Lyase (Prpb) From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of the 2-Methylisocitrate Lyase (Prpb) From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1002

b:43.3
occ:1.00
OD1 B:ASP87 2.2 28.7 1.0
O B:HOH1125 2.2 40.9 1.0
O B:HOH1058 2.3 26.9 1.0
O B:HOH1173 2.3 34.8 1.0
O B:HOH1047 2.3 31.5 1.0
CG B:ASP87 3.4 24.4 1.0
OD2 B:ASP58 3.7 31.2 1.0
OE1 B:GLU115 3.9 26.3 1.0
OD2 B:ASP85 3.9 24.1 1.0
OD2 B:ASP87 4.0 27.2 1.0
OE2 B:GLU115 4.0 28.7 1.0
OD1 B:ASP58 4.0 29.2 1.0
O B:HOH1072 4.1 40.7 1.0
CG B:ASP58 4.3 29.6 1.0
CD B:GLU115 4.3 26.1 1.0
OD1 B:ASP85 4.4 19.6 1.0
CB B:ASP87 4.5 23.7 1.0
CG B:ASP85 4.6 20.0 1.0
NH1 B:ARG158 4.7 28.3 1.0
CA B:ASP87 4.8 20.8 1.0
NH2 B:ARG158 4.9 28.7 1.0

Reference:

C.Grimm, A.Evers, M.Brock, C.Maerker, G.Klebe, W.Buckel, K.Reuter. Crystal Structure of 2-Methylisocitrate Lyase (Prpb) From Escherichia Coli and Modelling of Its Ligand Bound Active Centre. J.Mol.Biol. V. 328 609 2003.
ISSN: ISSN 0022-2836
PubMed: 12706720
DOI: 10.1016/S0022-2836(03)00358-9
Page generated: Mon Dec 14 06:29:39 2020

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