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Potassium in PDB 3s5n: Crystal Structure of Human 4-Hydroxy-2-Oxoglutarate Aldolase

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

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

Protein crystallography data

The structure of Crystal Structure of Human 4-Hydroxy-2-Oxoglutarate Aldolase, PDB code: 3s5n 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) 46.52 / 2.50
Space group P 64 2 2
Cell size a, b, c (Å), α, β, γ (°) 142.143, 142.143, 108.070, 90.00, 90.00, 120.00
R / Rfree (%) 21.2 / 24.6

Other elements in 3s5n:

The structure of Crystal Structure of Human 4-Hydroxy-2-Oxoglutarate Aldolase also contains other interesting chemical elements:

Sodium (Na) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Human 4-Hydroxy-2-Oxoglutarate Aldolase (pdb code 3s5n). 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, PDB code: 3s5n:

Potassium binding site 1 out of 1 in 3s5n

Go back to Potassium Binding Sites List in 3s5n
Potassium binding site 1 out of 1 in the Crystal Structure of Human 4-Hydroxy-2-Oxoglutarate Aldolase


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K330

b:44.1
occ:1.00
O A:SER187 2.6 41.9 1.0
O A:HOH370 2.6 43.2 1.0
O A:HIS189 2.7 42.2 1.0
O A:ASP216 2.7 42.4 1.0
O A:ILE192 2.7 35.2 1.0
O A:HOH353 3.0 37.3 1.0
C A:SER187 3.7 41.7 1.0
C A:HIS189 3.8 41.8 1.0
C A:ASP216 3.8 42.5 1.0
C A:ILE192 3.9 35.5 1.0
CB A:ASP216 4.3 44.0 1.0
N A:HIS189 4.4 42.3 1.0
N A:ASP216 4.4 44.0 1.0
CA A:ASP216 4.4 43.6 1.0
C A:GLN188 4.4 43.0 1.0
CA A:SER187 4.5 40.6 1.0
CA A:PRO190 4.5 40.7 1.0
N A:ILE192 4.6 35.7 1.0
N A:PRO190 4.6 41.5 1.0
O A:PRO190 4.6 39.9 1.0
C A:PRO190 4.6 39.9 1.0
N A:GLN188 4.6 42.4 1.0
CA A:ILE192 4.7 35.3 1.0
CA A:VAL193 4.7 35.6 1.0
CA A:HIS189 4.7 41.6 1.0
N A:VAL193 4.7 35.3 1.0
O A:GLN188 4.7 43.8 1.0
CA A:GLN188 4.8 43.5 1.0
CB A:GLN215 4.8 45.0 1.0
N A:PHE217 4.9 41.1 1.0
CB A:ILE192 4.9 35.1 1.0
CD2 A:PHE217 4.9 38.0 1.0
OE1 A:GLN215 4.9 39.7 1.0
CB A:PHE217 5.0 39.5 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 23:22:45 2020

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