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Potassium in PDB 3s5o: Crystal Structure of Human 4-Hydroxy-2-Oxoglutarate Aldolase Bound to Pyruvate

Enzymatic activity of Crystal Structure of Human 4-Hydroxy-2-Oxoglutarate Aldolase Bound to Pyruvate

All present enzymatic activity of Crystal Structure of Human 4-Hydroxy-2-Oxoglutarate Aldolase Bound to Pyruvate:
4.1.3.16;

Protein crystallography data

The structure of Crystal Structure of Human 4-Hydroxy-2-Oxoglutarate Aldolase Bound to Pyruvate, PDB code: 3s5o was solved by T.J.Riedel, W.T.Lowther, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.65 / 1.97
Space group P 64 2 2
Cell size a, b, c (Å), α, β, γ (°) 141.230, 141.230, 108.388, 90.00, 90.00, 120.00
R / Rfree (%) 19.6 / 21.6

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Human 4-Hydroxy-2-Oxoglutarate Aldolase Bound to Pyruvate (pdb code 3s5o). 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 Crystal Structure of Human 4-Hydroxy-2-Oxoglutarate Aldolase Bound to Pyruvate, PDB code: 3s5o:

Potassium binding site 1 out of 1 in 3s5o

Go back to Potassium Binding Sites List in 3s5o
Potassium binding site 1 out of 1 in the Crystal Structure of Human 4-Hydroxy-2-Oxoglutarate Aldolase Bound to Pyruvate


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of Human 4-Hydroxy-2-Oxoglutarate Aldolase Bound to Pyruvate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K328

b:29.0
occ:1.00
O A:ILE192 2.6 22.9 1.0
O A:SER187 2.7 27.0 1.0
O A:HIS189 2.7 29.3 1.0
O A:ASP216 2.7 25.9 1.0
O A:HOH371 2.7 28.3 1.0
O A:HOH342 3.0 28.1 1.0
C A:ILE192 3.7 23.3 1.0
C A:SER187 3.8 27.6 1.0
C A:HIS189 3.8 30.0 1.0
C A:ASP216 3.8 27.5 1.0
N A:HIS189 4.4 30.1 1.0
CB A:ASP216 4.4 29.3 1.0
N A:ASP216 4.4 29.2 1.0
C A:GLN188 4.4 30.2 1.0
N A:ILE192 4.4 25.0 1.0
CA A:ASP216 4.5 29.0 1.0
CA A:PRO190 4.5 29.9 1.0
CA A:VAL193 4.5 23.9 1.0
CA A:SER187 4.5 26.7 1.0
N A:VAL193 4.6 23.6 1.0
CA A:ILE192 4.6 23.6 1.0
O A:PRO190 4.6 29.8 1.0
C A:PRO190 4.6 29.6 1.0
N A:PRO190 4.6 30.1 1.0
N A:GLN188 4.7 28.6 1.0
O A:GLN188 4.7 30.5 1.0
CA A:HIS189 4.7 30.0 1.0
CA A:GLN188 4.8 30.1 1.0
CB A:GLN215 4.9 30.3 1.0
N A:PHE217 4.9 26.1 1.0
CB A:ILE192 4.9 23.5 1.0
OE1 A:GLN215 5.0 29.8 1.0
O A:LEU186 5.0 25.0 1.0

Reference:

T.J.Riedel, L.C.Johnson, J.Knight, R.R.Hantgan, R.P.Holmes, W.T.Lowther. Structural and Biochemical Studies of Human 4-Hydroxy-2-Oxoglutarate Aldolase: Implications For Hydroxyproline Metabolism in Primary Hyperoxaluria. Plos One V. 6 26021 2011.
ISSN: ESSN 1932-6203
PubMed: 21998747
DOI: 10.1371/JOURNAL.PONE.0026021
Page generated: Sun Dec 13 23:22:47 2020

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