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Potassium in PDB 1w5p: Stepwise Introduction of Zinc Binding Site Into Porphobilinogen Synthase of Pseudomonas Aeruginosa (Mutations A129C, D131C, D139C, P132E)

Enzymatic activity of Stepwise Introduction of Zinc Binding Site Into Porphobilinogen Synthase of Pseudomonas Aeruginosa (Mutations A129C, D131C, D139C, P132E)

All present enzymatic activity of Stepwise Introduction of Zinc Binding Site Into Porphobilinogen Synthase of Pseudomonas Aeruginosa (Mutations A129C, D131C, D139C, P132E):
4.2.1.24;

Protein crystallography data

The structure of Stepwise Introduction of Zinc Binding Site Into Porphobilinogen Synthase of Pseudomonas Aeruginosa (Mutations A129C, D131C, D139C, P132E), PDB code: 1w5p 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) 91.29 / 1.55
Space group P 4 21 2
Cell size a, b, c (Å), α, β, γ (°) 126.970, 126.970, 86.432, 90.00, 90.00, 90.00
R / Rfree (%) 15.7 / 18.5

Other elements in 1w5p:

The structure of Stepwise Introduction of Zinc Binding Site Into Porphobilinogen Synthase of Pseudomonas Aeruginosa (Mutations A129C, D131C, D139C, P132E) also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms
Zinc (Zn) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Stepwise Introduction of Zinc Binding Site Into Porphobilinogen Synthase of Pseudomonas Aeruginosa (Mutations A129C, D131C, D139C, P132E) (pdb code 1w5p). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Stepwise Introduction of Zinc Binding Site Into Porphobilinogen Synthase of Pseudomonas Aeruginosa (Mutations A129C, D131C, D139C, P132E), PDB code: 1w5p:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 1w5p

Go back to Potassium Binding Sites List in 1w5p
Potassium binding site 1 out of 2 in the Stepwise Introduction of Zinc Binding Site Into Porphobilinogen Synthase of Pseudomonas Aeruginosa (Mutations A129C, D131C, D139C, P132E)


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Stepwise Introduction of Zinc Binding Site Into Porphobilinogen Synthase of Pseudomonas Aeruginosa (Mutations A129C, D131C, D139C, P132E) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1341

b:27.1
occ:0.70
O A:ARG26 2.8 15.4 0.8
O A:ARG26 2.9 15.8 0.2
O A:LEU27 3.1 15.8 1.0
O A:HOH2028 3.2 18.1 1.0
C A:LEU27 3.6 15.0 1.0
CA A:LEU27 3.8 14.8 1.0
C A:ARG26 3.9 14.6 0.8
C A:ARG26 4.0 15.5 0.2
O A:ARG29 4.0 15.8 1.0
N A:LEU27 4.4 14.6 1.0
N A:ARG29 4.5 14.7 1.0
N A:VAL28 4.6 14.1 1.0
CB A:ARG29 4.9 16.5 1.0
C A:ARG29 5.0 15.1 1.0

Potassium binding site 2 out of 2 in 1w5p

Go back to Potassium Binding Sites List in 1w5p
Potassium binding site 2 out of 2 in the Stepwise Introduction of Zinc Binding Site Into Porphobilinogen Synthase of Pseudomonas Aeruginosa (Mutations A129C, D131C, D139C, P132E)


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Stepwise Introduction of Zinc Binding Site Into Porphobilinogen Synthase of Pseudomonas Aeruginosa (Mutations A129C, D131C, D139C, P132E) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K1340

b:25.9
occ:0.70
O B:ARG26 2.8 15.6 0.5
O B:ARG26 2.9 13.8 0.5
O B:HOH2031 3.1 16.9 1.0
O B:LEU27 3.1 14.7 1.0
O2 B:GOL1343 3.3 35.0 0.5
C2 B:GOL1343 3.6 34.7 0.5
C B:LEU27 3.6 14.1 1.0
O3 B:GOL1343 3.7 35.1 0.5
CA B:LEU27 3.8 13.6 1.0
C B:ARG26 3.9 15.1 0.5
C B:ARG26 4.0 12.9 0.5
O B:ARG29 4.0 14.8 1.0
O1 B:GOL1343 4.1 36.9 0.5
O2 B:GOL1343 4.2 39.4 0.5
C2 B:GOL1343 4.3 38.8 0.5
C3 B:GOL1343 4.3 34.9 0.5
N B:LEU27 4.4 13.7 1.0
N B:ARG29 4.5 13.7 1.0
N B:VAL28 4.5 13.2 1.0
C1 B:GOL1343 4.8 38.5 0.5
C1 B:GOL1343 4.8 34.7 0.5
CB B:ARG29 4.8 15.2 1.0
O1 B:GOL1343 4.9 34.1 0.5
C B:ARG29 4.9 14.6 1.0
C B:VAL28 5.0 15.1 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: Mon Aug 12 05:43:08 2024

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