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Potassium in PDB 3q1y: Allosteric Regulation By Lysine Residue: A Novel Anion-Hole Formation in the Ribokinase Family

Enzymatic activity of Allosteric Regulation By Lysine Residue: A Novel Anion-Hole Formation in the Ribokinase Family

All present enzymatic activity of Allosteric Regulation By Lysine Residue: A Novel Anion-Hole Formation in the Ribokinase Family:
2.7.1.144;

Protein crystallography data

The structure of Allosteric Regulation By Lysine Residue: A Novel Anion-Hole Formation in the Ribokinase Family, PDB code: 3q1y was solved by L.Satyanarayana, S.K.Burley, S.Swaminathan, New York Sgx Research Centerfor Structural Genomics (Nysgxrc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.03
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 88.912, 44.717, 87.955, 90.00, 113.48, 90.00
R / Rfree (%) 18.8 / 22.8

Potassium Binding Sites:

The binding sites of Potassium atom in the Allosteric Regulation By Lysine Residue: A Novel Anion-Hole Formation in the Ribokinase Family (pdb code 3q1y). 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 Allosteric Regulation By Lysine Residue: A Novel Anion-Hole Formation in the Ribokinase Family, PDB code: 3q1y:

Potassium binding site 1 out of 1 in 3q1y

Go back to Potassium Binding Sites List in 3q1y
Potassium binding site 1 out of 1 in the Allosteric Regulation By Lysine Residue: A Novel Anion-Hole Formation in the Ribokinase Family


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Allosteric Regulation By Lysine Residue: A Novel Anion-Hole Formation in the Ribokinase Family within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1

b:28.6
occ:1.00
 O A:ASP286 2.5 39.1 1.0
O A:ALA281 2.8 25.5 1.0
O A:ASN245 2.9 33.0 1.0
O A:GLN284 3.1 34.4 1.0
O A:THR247 3.4 29.2 1.0
C A:ASP286 3.6 39.2 1.0
C A:ALA281 3.8 25.7 1.0
C A:GLN284 4.0 34.9 1.0
C A:ASN245 4.0 33.4 1.0
O A:SER287 4.0 40.4 1.0
C A:SER287 4.1 39.7 1.0
OD1 A:ASP286 4.1 40.2 1.0
CA A:SER287 4.2 40.0 1.0
N A:SER287 4.3 39.6 1.0
CB A:GLN284 4.3 33.9 1.0
CB A:ASN245 4.4 34.2 1.0
N A:ASP286 4.4 38.3 1.0
C A:THR247 4.5 28.7 1.0
CA A:GLN284 4.6 34.0 1.0
CA A:ASP286 4.6 38.8 1.0
CA A:ALA281 4.6 25.3 1.0
N A:VAL282 4.6 26.6 1.0
C A:GLN285 4.6 37.8 1.0
O A:SER289 4.6 34.6 1.0
CB A:ALA281 4.6 24.6 1.0
CG A:ASN245 4.6 34.4 1.0
N A:GLN284 4.7 33.0 1.0
CA A:VAL282 4.7 28.1 1.0
N A:SER288 4.7 39.1 1.0
N A:THR247 4.7 30.3 1.0
CA A:ASN245 4.8 34.2 1.0
ND2 A:ASN245 4.8 35.6 1.0
O A:GLN285 4.8 38.3 1.0
C A:ASP246 4.9 31.4 1.0
N A:GLN285 4.9 36.0 1.0
N A:ASP246 4.9 32.7 1.0
C A:VAL282 5.0 28.9 1.0

Reference:

L.Satyanarayan, S.K.Burley, S.Swaminathan. Allosteric Regulation By Lysine Residue: A Novel Anion-Hole Formation in the Ribokinase Family To Be Published.
Page generated: Mon Aug 12 09:05:21 2024

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