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Potassium in PDB 4pyo: Humanized Rat Comt Bound to Sah, Semi-Holo Form

Enzymatic activity of Humanized Rat Comt Bound to Sah, Semi-Holo Form

All present enzymatic activity of Humanized Rat Comt Bound to Sah, Semi-Holo Form:
2.1.1.6;

Protein crystallography data

The structure of Humanized Rat Comt Bound to Sah, Semi-Holo Form, PDB code: 4pyo 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) 45.88 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 58.369, 60.380, 148.415, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / 23.3

Other elements in 4pyo:

The structure of Humanized Rat Comt Bound to Sah, Semi-Holo Form also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Humanized Rat Comt Bound to Sah, Semi-Holo Form (pdb code 4pyo). 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 Humanized Rat Comt Bound to Sah, Semi-Holo Form, PDB code: 4pyo:

Potassium binding site 1 out of 1 in 4pyo

Go back to Potassium Binding Sites List in 4pyo
Potassium binding site 1 out of 1 in the Humanized Rat Comt Bound to Sah, Semi-Holo Form


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Humanized Rat Comt Bound to Sah, Semi-Holo Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K302

b:67.3
occ:1.00
O A:VAL226 2.5 36.0 1.0
O A:PHE232 2.5 50.5 1.0
O A:ARG227 2.6 43.7 1.0
O A:HOH440 2.6 48.6 1.0
O A:SER229 2.6 41.0 1.0
O A:HOH411 2.7 40.1 1.0
C A:ARG227 3.1 43.0 1.0
CA A:ARG227 3.4 41.8 1.0
C A:PHE232 3.6 46.6 1.0
C A:VAL226 3.6 42.0 1.0
C A:SER229 3.7 44.8 1.0
N A:SER229 3.7 38.4 1.0
N A:GLY228 4.0 44.0 1.0
N A:ARG227 4.0 40.8 1.0
SG A:CYS234 4.2 45.9 1.0
CA A:SER229 4.2 44.7 1.0
C A:GLY228 4.2 42.1 1.0
CA A:PHE232 4.3 44.9 1.0
CB A:PHE232 4.3 42.0 1.0
N A:PHE232 4.4 39.2 1.0
N A:GLU233 4.5 44.1 1.0
CA A:GLY228 4.6 40.1 1.0
CA A:GLU233 4.6 46.7 1.0
OE2 A:GLU233 4.6 91.5 1.0
N A:SER230 4.7 50.4 1.0
O A:HOH448 4.7 57.0 1.0
CB A:ARG227 4.8 39.4 1.0
CB A:SER229 4.8 48.3 1.0
N A:CYS234 4.9 39.9 1.0
CA A:VAL226 4.9 39.6 1.0
CD A:GLU233 5.0 86.5 1.0
O A:GLY228 5.0 45.9 1.0
CA A:SER230 5.0 53.5 1.0
OE1 A:GLU233 5.0 88.5 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: ISSN 0907-4449
PubMed: 25084335
DOI: 10.1107/S1399004714012917
Page generated: Sun Dec 13 23:47:56 2020

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