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Potassium in PDB 4p7j: Rat Apo-Comt Sulfate Bound

Enzymatic activity of Rat Apo-Comt Sulfate Bound

All present enzymatic activity of Rat Apo-Comt Sulfate Bound:
2.1.1.6;

Protein crystallography data

The structure of Rat Apo-Comt Sulfate Bound, PDB code: 4p7j was solved by A.Ehler, J.Benz, D.Schlatter, M.G.Rudolph, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.10 / 1.45
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 56.286, 56.286, 119.082, 90.00, 90.00, 120.00
R / Rfree (%) 16.7 / 19.8

Potassium Binding Sites:

The binding sites of Potassium atom in the Rat Apo-Comt Sulfate Bound (pdb code 4p7j). 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 Rat Apo-Comt Sulfate Bound, PDB code: 4p7j:

Potassium binding site 1 out of 1 in 4p7j

Go back to Potassium Binding Sites List in 4p7j
Potassium binding site 1 out of 1 in the Rat Apo-Comt Sulfate Bound


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Rat Apo-Comt Sulfate Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K300

b:16.6
occ:1.00
O A:SER229 2.4 10.8 1.0
O A:VAL226 2.5 9.7 1.0
O A:PHE232 2.5 10.3 1.0
O A:ARG227 2.6 12.7 1.0
C A:ARG227 3.1 10.5 1.0
C A:SER229 3.4 10.8 1.0
CA A:ARG227 3.5 10.1 1.0
C A:VAL226 3.6 10.2 1.0
N A:SER229 3.6 11.1 1.0
C A:PHE232 3.6 10.4 1.0
CA A:SER229 4.0 10.2 1.0
N A:ARG227 4.0 10.3 1.0
N A:GLY228 4.1 10.3 1.0
C A:GLY228 4.1 12.5 1.0
CB A:PHE232 4.3 10.4 1.0
CA A:PHE232 4.3 10.6 1.0
N A:PHE232 4.3 10.1 1.0
SG A:CYS234 4.4 11.6 1.0
CB A:SER229 4.5 12.8 1.0
N A:SER230 4.5 10.7 1.0
CA A:GLY228 4.6 11.1 1.0
N A:GLU233 4.7 9.9 1.0
O A:GLY228 4.7 12.4 1.0
CA A:SER230 4.8 11.1 1.0
CA A:VAL226 4.9 9.4 1.0
CB A:ARG227 4.9 12.0 1.0

Reference:

A.Ehler, J.Benz, D.Schlatter, M.G.Rudolph. Mapping the Conformational Space Accessible to Catechol-O-Methyltransferase. Acta Crystallogr.,Sect.D V. 70 2163 2014.
ISSN: ESSN 1399-0047
PubMed: 25084335
DOI: 10.1107/S1399004714012917
Page generated: Sun Dec 13 23:46:44 2020

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