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Potassium in PDB 1m0q: Structure of Dialkylglycine Decarboxylase Complexed with S-1- Aminoethanephosphonate

Enzymatic activity of Structure of Dialkylglycine Decarboxylase Complexed with S-1- Aminoethanephosphonate

All present enzymatic activity of Structure of Dialkylglycine Decarboxylase Complexed with S-1- Aminoethanephosphonate:
4.1.1.64;

Protein crystallography data

The structure of Structure of Dialkylglycine Decarboxylase Complexed with S-1- Aminoethanephosphonate, PDB code: 1m0q was solved by W.Liu, C.J.Rogers, A.J.Fisher, M.D.Toney, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.00
Space group P 64 2 2
Cell size a, b, c (Å), α, β, γ (°) 150.810, 150.810, 85.050, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Other elements in 1m0q:

The structure of Structure of Dialkylglycine Decarboxylase Complexed with S-1- Aminoethanephosphonate also contains other interesting chemical elements:

Sodium (Na) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Structure of Dialkylglycine Decarboxylase Complexed with S-1- Aminoethanephosphonate (pdb code 1m0q). 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 Structure of Dialkylglycine Decarboxylase Complexed with S-1- Aminoethanephosphonate, PDB code: 1m0q:

Potassium binding site 1 out of 1 in 1m0q

Go back to Potassium Binding Sites List in 1m0q
Potassium binding site 1 out of 1 in the Structure of Dialkylglycine Decarboxylase Complexed with S-1- Aminoethanephosphonate


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of Dialkylglycine Decarboxylase Complexed with S-1- Aminoethanephosphonate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K434

b:27.3
occ:1.00
 O A:LEU78 2.6 28.0 1.0
OD1 A:ASP307 2.6 28.6 1.0
O A:VAL305 2.7 20.4 1.0
OG A:SER80 2.7 28.8 1.0
O A:HOH525 2.8 27.5 1.0
O A:THR303 2.8 24.0 1.0
CG A:ASP307 3.6 37.7 1.0
CA A:SER80 3.6 30.2 1.0
CB A:SER80 3.8 24.0 1.0
C A:LEU78 3.8 35.3 1.0
N A:SER80 3.8 24.8 1.0
C A:THR303 3.9 27.5 1.0
C A:VAL305 3.9 21.9 1.0
C A:HIS304 4.0 29.4 1.0
CA A:HIS304 4.1 23.2 1.0
C A:PHE79 4.1 26.8 1.0
N A:VAL305 4.2 23.7 1.0
OD2 A:ASP307 4.2 36.5 1.0
CE1 A:HIS77 4.3 22.4 1.0
O A:PHE79 4.3 22.8 1.0
N A:ASP307 4.3 34.8 1.0
C A:SER306 4.3 37.2 1.0
O A:SER306 4.3 25.5 1.0
CA A:ASP307 4.4 24.8 1.0
O A:HIS304 4.4 25.8 1.0
N A:HIS304 4.4 20.4 1.0
N A:LEU78 4.5 32.8 1.0
CB A:ASP307 4.5 24.5 1.0
ND1 A:HIS77 4.5 19.7 1.0
CA A:LEU78 4.6 30.2 1.0
CG1 A:VAL305 4.7 25.6 1.0
O A:THR302 4.8 27.2 1.0
N A:PHE79 4.8 32.4 1.0
CA A:VAL305 4.8 21.4 1.0
N A:SER306 4.9 27.0 1.0
CA A:PHE79 4.9 31.4 1.0
CA A:SER306 4.9 29.4 1.0
CB A:SER306 4.9 23.9 1.0
CB A:LEU78 5.0 26.9 1.0
C A:SER80 5.0 39.8 1.0

Reference:

W.Liu, C.J.Rogers, A.J.Fisher, M.D.Toney. Aminophosphonate Inhibitors of Dialkylglycine Decarboxylase: Structural Basis For Slow Binding Inhibition Biochemistry V. 41 12320 2002.
ISSN: ISSN 0006-2960
PubMed: 12369820
DOI: 10.1021/BI026318G
Page generated: Mon Aug 12 04:53:37 2024

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