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Potassium in PDB 3bwm: Crystal Structure of Human Catechol O-Methyltransferase with Bound Sam and Dnc

Enzymatic activity of Crystal Structure of Human Catechol O-Methyltransferase with Bound Sam and Dnc

All present enzymatic activity of Crystal Structure of Human Catechol O-Methyltransferase with Bound Sam and Dnc:
2.1.1.6;

Protein crystallography data

The structure of Crystal Structure of Human Catechol O-Methyltransferase with Bound Sam and Dnc, PDB code: 3bwm was solved by K.Rutherford, I.Le Trong, R.E.Stenkamp, W.W.Parson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.31 / 1.98
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 43.284, 66.648, 68.046, 90.00, 90.00, 90.00
R / Rfree (%) 17.5 / 22.5

Other elements in 3bwm:

The structure of Crystal Structure of Human Catechol O-Methyltransferase with Bound Sam and Dnc also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Human Catechol O-Methyltransferase with Bound Sam and Dnc (pdb code 3bwm). 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 Catechol O-Methyltransferase with Bound Sam and Dnc, PDB code: 3bwm:

Potassium binding site 1 out of 1 in 3bwm

Go back to Potassium Binding Sites List in 3bwm
Potassium binding site 1 out of 1 in the Crystal Structure of Human Catechol O-Methyltransferase with Bound Sam and Dnc


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 Catechol O-Methyltransferase with Bound Sam and Dnc within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K303

b:39.5
occ:1.00
 O A:SER186 2.5 36.7 1.0
O A:PHE189 2.6 33.0 1.0
O A:HOH425 2.8 18.3 0.5
O A:ARG184 2.9 32.0 1.0
O A:HOH426 2.9 51.3 1.0
O A:VAL183 3.0 30.4 1.0
C A:ARG184 3.5 32.0 1.0
C A:SER186 3.6 36.4 1.0
C A:PHE189 3.8 32.8 1.0
N A:SER186 3.9 35.1 1.0
CA A:ARG184 3.9 31.6 1.0
C A:VAL183 4.1 30.8 1.0
CA A:SER186 4.3 35.6 1.0
C A:GLY185 4.3 34.3 1.0
N A:GLY185 4.4 32.7 1.0
CA A:PHE189 4.5 33.3 1.0
N A:PHE189 4.5 34.3 1.0
N A:ARG184 4.5 30.9 1.0
CB A:PHE189 4.5 32.9 1.0
N A:SER187 4.6 37.2 1.0
SG A:CYS191 4.6 32.9 1.0
N A:GLU190 4.7 32.6 1.0
CA A:GLY185 4.8 33.6 1.0
CA A:SER187 4.8 37.9 1.0
O A:GLY185 4.8 34.8 1.0
CA A:GLU190 4.9 32.8 1.0
CB A:SER186 5.0 35.7 1.0

Reference:

K.Rutherford, I.Le Trong, R.E.Stenkamp, W.W.Parson. Crystal Structures of Human 108V and 108M Catechol O-Methyltransferase. J.Mol.Biol. V. 380 120 2008.
ISSN: ISSN 0022-2836
PubMed: 18486144
DOI: 10.1016/J.JMB.2008.04.040
Page generated: Mon Aug 12 07:51:46 2024

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