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Potassium in PDB 1gzg: Complex of A MG2-Dependent Porphobilinogen Synthase From Pseudomonas Aeruginosa (Mutant D139N) with 5-Fluorolevulinic Acid

Enzymatic activity of Complex of A MG2-Dependent Porphobilinogen Synthase From Pseudomonas Aeruginosa (Mutant D139N) with 5-Fluorolevulinic Acid

All present enzymatic activity of Complex of A MG2-Dependent Porphobilinogen Synthase From Pseudomonas Aeruginosa (Mutant D139N) with 5-Fluorolevulinic Acid:
4.2.1.24;

Protein crystallography data

The structure of Complex of A MG2-Dependent Porphobilinogen Synthase From Pseudomonas Aeruginosa (Mutant D139N) with 5-Fluorolevulinic Acid, PDB code: 1gzg was solved by F.Frere, W.-D.Schubert, F.Stauffer, N.Frankenberg, R.Neier, D.Jahn, D.W.Heinz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 91.29 / 1.66
Space group P 4 21 2
Cell size a, b, c (Å), α, β, γ (°) 127.131, 127.131, 86.145, 90.00, 90.00, 90.00
R / Rfree (%) 17.5 / 19.8

Other elements in 1gzg:

The structure of Complex of A MG2-Dependent Porphobilinogen Synthase From Pseudomonas Aeruginosa (Mutant D139N) with 5-Fluorolevulinic Acid also contains other interesting chemical elements:

Fluorine (F) 6 atoms
Magnesium (Mg) 2 atoms
Sodium (Na) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Complex of A MG2-Dependent Porphobilinogen Synthase From Pseudomonas Aeruginosa (Mutant D139N) with 5-Fluorolevulinic Acid (pdb code 1gzg). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Complex of A MG2-Dependent Porphobilinogen Synthase From Pseudomonas Aeruginosa (Mutant D139N) with 5-Fluorolevulinic Acid, PDB code: 1gzg:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 1gzg

Go back to Potassium Binding Sites List in 1gzg
Potassium binding site 1 out of 2 in the Complex of A MG2-Dependent Porphobilinogen Synthase From Pseudomonas Aeruginosa (Mutant D139N) with 5-Fluorolevulinic Acid


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Complex of A MG2-Dependent Porphobilinogen Synthase From Pseudomonas Aeruginosa (Mutant D139N) with 5-Fluorolevulinic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K1339

b:25.6
occ:1.00
OD1 B:ASP37 2.7 19.5 1.0
O B:ASP319 2.7 18.4 1.0
O B:ASP36 3.2 19.7 1.0
C B:ASP36 3.8 19.1 1.0
C B:ASP319 3.8 17.7 1.0
CG B:ASP37 3.9 18.8 1.0
CA B:ASP37 3.9 18.4 1.0
NZ B:LYS314 4.0 13.9 0.2
N B:ASP37 4.1 19.0 1.0
O B:HOH2081 4.3 29.4 1.0
CB B:ASP36 4.3 21.0 1.0
O B:HOH2302 4.4 34.6 1.0
CB B:ASP37 4.4 18.3 1.0
CA B:ASP319 4.4 17.6 1.0
O B:HOH2087 4.6 58.6 1.0
CB B:ASP319 4.7 17.3 1.0
CA B:ASP36 4.7 20.1 1.0
OD2 B:ASP37 4.8 17.1 1.0
N B:GLY320 4.9 17.6 1.0

Potassium binding site 2 out of 2 in 1gzg

Go back to Potassium Binding Sites List in 1gzg
Potassium binding site 2 out of 2 in the Complex of A MG2-Dependent Porphobilinogen Synthase From Pseudomonas Aeruginosa (Mutant D139N) with 5-Fluorolevulinic Acid


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Complex of A MG2-Dependent Porphobilinogen Synthase From Pseudomonas Aeruginosa (Mutant D139N) with 5-Fluorolevulinic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K1340

b:23.6
occ:1.00
O B:HOH2066 2.7 36.7 1.0
O B:LEU27 2.7 15.5 1.0
O B:HOH2067 2.9 23.2 1.0
O B:ARG26 3.2 15.9 1.0
C B:LEU27 3.4 14.9 1.0
CA B:LEU27 3.8 14.8 1.0
O B:ARG29 4.0 16.4 1.0
C B:ARG26 4.2 15.1 1.0
N B:VAL28 4.4 14.5 1.0
N B:ARG29 4.5 15.4 1.0
N B:LEU27 4.5 14.7 1.0
C B:VAL28 4.8 15.1 1.0
CA B:VAL28 4.9 14.3 1.0
C B:ARG29 4.9 16.0 1.0

Reference:

F.Frere, W.D.Schubert, F.Stauffer, N.Frankenberg, R.Neier, D.Jahn, D.W.Heinz. Structure of Porphobilinogen Synthase From Pseudomonas Aeruginosa in Complex with 5-Fluorolevulinic Acid Suggests A Double Schiff Base Mechanism. J. Mol. Biol. V. 320 237 2002.
ISSN: ISSN 0022-2836
PubMed: 12079382
DOI: 10.1016/S0022-2836(02)00472-2
Page generated: Sun Dec 13 22:43:39 2020

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