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Potassium in PDB 1dka: Dialkylglycine Decarboxylase Structure: Bifunctional Active Site and Alkali Metal Binding Sites

Enzymatic activity of Dialkylglycine Decarboxylase Structure: Bifunctional Active Site and Alkali Metal Binding Sites

All present enzymatic activity of Dialkylglycine Decarboxylase Structure: Bifunctional Active Site and Alkali Metal Binding Sites:
4.1.1.64;

Protein crystallography data

The structure of Dialkylglycine Decarboxylase Structure: Bifunctional Active Site and Alkali Metal Binding Sites, PDB code: 1dka was solved by M.D.Toney, E.Hohenester, J.N.Jansonius, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.60
Space group P 64 2 2
Cell size a, b, c (Å), α, β, γ (°) 152.700, 152.700, 86.600, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Other elements in 1dka:

The structure of Dialkylglycine Decarboxylase Structure: Bifunctional Active Site and Alkali Metal Binding Sites also contains other interesting chemical elements:

Sodium (Na) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Dialkylglycine Decarboxylase Structure: Bifunctional Active Site and Alkali Metal Binding Sites (pdb code 1dka). 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 Dialkylglycine Decarboxylase Structure: Bifunctional Active Site and Alkali Metal Binding Sites, PDB code: 1dka:

Potassium binding site 1 out of 1 in 1dka

Go back to Potassium Binding Sites List in 1dka
Potassium binding site 1 out of 1 in the Dialkylglycine Decarboxylase Structure: Bifunctional Active Site and Alkali Metal Binding Sites


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Dialkylglycine Decarboxylase Structure: Bifunctional Active Site and Alkali Metal Binding Sites within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K436

b:13.5
occ:1.00
 OD1 A:ASP307 2.5 13.4 1.0
O A:LEU78 2.7 16.5 1.0
O A:HOH530 2.7 23.6 1.0
O A:THR303 2.7 24.2 1.0
OG A:SER80 2.8 24.6 1.0
O A:VAL305 2.9 17.8 1.0
CG A:ASP307 3.5 18.6 1.0
N A:SER80 3.8 18.1 1.0
CA A:SER80 3.8 23.6 1.0
C A:THR303 3.8 21.1 1.0
C A:LEU78 3.8 13.2 1.0
CB A:SER80 3.8 24.3 1.0
C A:VAL305 4.0 17.4 1.0
C A:PHE79 4.1 17.9 1.0
C A:HIS304 4.1 13.5 1.0
N A:VAL305 4.1 11.6 1.0
CA A:HIS304 4.1 12.8 1.0
OD2 A:ASP307 4.2 13.9 1.0
CE1 A:HIS77 4.2 12.9 1.0
CG1 A:VAL305 4.2 5.0 1.0
O A:SER306 4.3 15.9 1.0
ND1 A:HIS77 4.3 12.1 1.0
O A:PHE79 4.3 15.2 1.0
N A:HIS304 4.4 19.2 1.0
C A:SER306 4.4 17.3 1.0
N A:LEU78 4.4 9.3 1.0
N A:ASP307 4.5 18.0 1.0
CB A:ASP307 4.5 17.2 1.0
CA A:ASP307 4.6 20.3 1.0
O A:HIS304 4.6 7.2 1.0
CA A:LEU78 4.6 14.0 1.0
O A:THR302 4.7 18.2 1.0
N A:PHE79 4.7 18.4 1.0
CA A:VAL305 4.7 14.7 1.0
CA A:PHE79 4.7 16.0 1.0
CA A:THR303 5.0 15.4 1.0
N A:SER306 5.0 21.4 1.0

Reference:

M.D.Toney, E.Hohenester, S.W.Cowan, J.N.Jansonius. Dialkylglycine Decarboxylase Structure: Bifunctional Active Site and Alkali Metal Sites. Science V. 261 756 1993.
ISSN: ISSN 0036-8075
PubMed: 8342040
Page generated: Mon Aug 12 04:24:14 2024

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