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Magnesium in PDB 1w54: Stepwise Introduction of A Zinc Binding Site Into Porphobilinogen Synthase From Pseudomonas Aeruginosa (Mutation D139C)

Enzymatic activity of Stepwise Introduction of A Zinc Binding Site Into Porphobilinogen Synthase From Pseudomonas Aeruginosa (Mutation D139C)

All present enzymatic activity of Stepwise Introduction of A Zinc Binding Site Into Porphobilinogen Synthase From Pseudomonas Aeruginosa (Mutation D139C):
4.2.1.24;

Protein crystallography data

The structure of Stepwise Introduction of A Zinc Binding Site Into Porphobilinogen Synthase From Pseudomonas Aeruginosa (Mutation D139C), PDB code: 1w54 was solved by F.Frere, H.Reents, W.-D.Schubert, D.W.Heinz, D.Jahn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 87.71 / 2.20
Space group P 4 21 2
Cell size a, b, c (Å), α, β, γ (°) 125.231, 125.232, 86.030, 90.00, 90.00, 90.00
R / Rfree (%) 15.4 / 21.7

Other elements in 1w54:

The structure of Stepwise Introduction of A Zinc Binding Site Into Porphobilinogen Synthase From Pseudomonas Aeruginosa (Mutation D139C) also contains other interesting chemical elements:

Potassium (K) 2 atoms
Zinc (Zn) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Stepwise Introduction of A Zinc Binding Site Into Porphobilinogen Synthase From Pseudomonas Aeruginosa (Mutation D139C) (pdb code 1w54). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Stepwise Introduction of A Zinc Binding Site Into Porphobilinogen Synthase From Pseudomonas Aeruginosa (Mutation D139C), PDB code: 1w54:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1w54

Go back to Magnesium Binding Sites List in 1w54
Magnesium binding site 1 out of 2 in the Stepwise Introduction of A Zinc Binding Site Into Porphobilinogen Synthase From Pseudomonas Aeruginosa (Mutation D139C)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Stepwise Introduction of A Zinc Binding Site Into Porphobilinogen Synthase From Pseudomonas Aeruginosa (Mutation D139C) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1339

b:20.6
occ:1.00
O A:HOH2134 2.0 25.0 1.0
OE1 A:GLU245 2.0 20.5 1.0
O A:HOH2135 2.0 20.9 1.0
O A:HOH2136 2.1 20.9 1.0
O A:HOH2133 2.1 17.2 1.0
O A:HOH2108 2.2 21.0 1.0
CD A:GLU245 3.1 19.8 1.0
OE2 A:GLU245 3.4 21.7 1.0
OD1 A:ASP249 3.8 19.8 1.0
NH1 A:ARG181 3.8 33.9 1.0
O A:HOH2107 4.0 33.6 1.0
O A:HOH2140 4.2 19.3 1.0
OD2 A:ASP249 4.2 16.6 1.0
O A:HOH2138 4.3 19.4 1.0
O A:MET178 4.4 21.2 1.0
CG A:GLU245 4.4 13.9 1.0
CG A:ASP249 4.4 22.1 1.0
O A:SER203 4.4 22.1 1.0
OD1 A:ASP179 4.5 21.6 1.0
O A:GLU245 4.5 11.9 1.0
CB A:GLU245 4.6 19.4 1.0
CA A:GLU245 4.7 14.8 1.0
CA A:ASP179 4.7 21.3 1.0
O B:HOH2009 4.8 32.8 1.0
SD A:MET177 4.8 24.8 1.0
CE A:MET177 4.8 27.7 1.0

Magnesium binding site 2 out of 2 in 1w54

Go back to Magnesium Binding Sites List in 1w54
Magnesium binding site 2 out of 2 in the Stepwise Introduction of A Zinc Binding Site Into Porphobilinogen Synthase From Pseudomonas Aeruginosa (Mutation D139C)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Stepwise Introduction of A Zinc Binding Site Into Porphobilinogen Synthase From Pseudomonas Aeruginosa (Mutation D139C) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1339

b:48.3
occ:1.00
O B:HOH2101 1.9 27.9 1.0
O B:HOH2100 2.4 47.8 1.0
OE1 B:GLU245 2.7 41.5 1.0
NH1 B:ARG181 3.5 60.3 1.0
OD1 B:ASP249 3.5 28.6 1.0
O B:MET178 3.8 60.9 1.0
CD B:GLU245 3.8 33.8 1.0
OD1 B:ASP179 3.8 68.8 1.0
OE2 B:GLU245 4.2 40.1 1.0
CA B:ASP179 4.3 55.9 1.0
OD2 B:ASP249 4.3 25.8 1.0
CG B:ASP249 4.4 23.4 1.0
C B:MET178 4.6 60.6 1.0
CZ B:ARG181 4.7 54.6 1.0
O B:GLU245 4.7 24.1 1.0
N B:ASP179 4.8 58.6 1.0
CG B:ASP179 4.8 63.8 1.0
N B:GLY180 4.9 50.0 1.0
CB B:ASP179 5.0 60.6 1.0

Reference:

F.Frere, H.Reents, W.-D.Schubert, D.W.Heinz, D.Jahn. Tracking the Evolution of Porphobilinogen Synthase Metal Dependence in Vitro J.Mol.Biol. V. 345 1059 2005.
ISSN: ISSN 0022-2836
PubMed: 15644204
DOI: 10.1016/J.JMB.2004.10.053
Page generated: Tue Aug 13 16:52:14 2024

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