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Potassium in PDB 8d2y: Y430F Mutant of D-Ornithine/D-Lysine Decarboxylase

Enzymatic activity of Y430F Mutant of D-Ornithine/D-Lysine Decarboxylase

All present enzymatic activity of Y430F Mutant of D-Ornithine/D-Lysine Decarboxylase:
4.1.1.116;

Protein crystallography data

The structure of Y430F Mutant of D-Ornithine/D-Lysine Decarboxylase, PDB code: 8d2y was solved by R.S.Phillips, K.N.Nguyen Hoang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.66 / 1.22
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 139.74, 50.74, 73.32, 90, 120.8, 90
R / Rfree (%) 13.4 / 15.2

Other elements in 8d2y:

The structure of Y430F Mutant of D-Ornithine/D-Lysine Decarboxylase also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Y430F Mutant of D-Ornithine/D-Lysine Decarboxylase (pdb code 8d2y). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Y430F Mutant of D-Ornithine/D-Lysine Decarboxylase, PDB code: 8d2y:

Potassium binding site 1 out of 1 in 8d2y

Go back to Potassium Binding Sites List in 8d2y
Potassium binding site 1 out of 1 in the Y430F Mutant of D-Ornithine/D-Lysine Decarboxylase


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Y430F Mutant of D-Ornithine/D-Lysine Decarboxylase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K512

b:16.2
occ:0.72
O A:VAL210 2.6 19.7 1.0
O A:MET207 2.6 20.9 1.0
O A:HOH827 2.8 49.4 1.0
O A:ILE204 2.8 18.5 1.0
O A:LEU205 2.9 24.2 1.0
O A:HOH1075 3.1 14.4 1.0
HA A:LEU205 3.1 23.8 1.0
C A:LEU205 3.4 21.7 1.0
H A:MET207 3.6 24.6 1.0
OXT A:ACT507 3.7 64.2 1.0
CA A:LEU205 3.7 19.8 1.0
C A:MET207 3.8 19.4 1.0
C A:VAL210 3.8 17.8 1.0
C A:ILE204 3.9 18.8 1.0
HB2 A:MET207 3.9 23.9 1.0
N A:MET207 3.9 20.4 1.0
H A:VAL210 3.9 20.5 1.0
HA A:HIS211 4.0 19.1 1.0
O A:ACT507 4.1 41.6 1.0
HG22 A:ILE204 4.3 19.3 1.0
C A:ACT507 4.3 66.3 1.0
N A:LEU205 4.3 20.1 1.0
CA A:MET207 4.3 19.5 1.0
N A:ALA206 4.3 23.2 1.0
HB A:VAL210 4.4 19.5 1.0
O A:HOH1077 4.5 43.4 1.0
H A:LEU212 4.5 19.5 1.0
O A:HOH1058 4.6 47.7 1.0
C A:ALA206 4.6 24.2 1.0
HG23 A:ILE204 4.6 19.3 1.0
CB A:MET207 4.6 19.8 1.0
N A:VAL210 4.6 17.1 1.0
HD23 A:LEU205 4.6 33.1 1.0
N A:HIS211 4.7 16.8 1.0
CA A:VAL210 4.7 16.7 1.0
CA A:HIS211 4.8 15.8 1.0
HA A:PRO208 4.8 23.7 1.0
N A:PRO208 4.9 19.8 1.0
CG2 A:ILE204 4.9 16.1 1.0
H A:ALA206 4.9 27.9 1.0
CA A:ALA206 4.9 24.4 1.0
O A:HOH912 4.9 35.1 1.0
HA A:ALA206 4.9 29.3 1.0

Reference:

R.S.Phillips, K.N.Nguyen Hoang. The Y430F Mutant of Salmonella D-Ornithine/D-Lysine Decarboxylase Has Altered Stereospecificity and A Putrescine Allosteric Activation Site. Arch.Biochem.Biophys. V. 731 09429 2022.
ISSN: ESSN 1096-0384
PubMed: 36265649
DOI: 10.1016/J.ABB.2022.109429
Page generated: Sat Aug 9 16:40:41 2025

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