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Fluorine in PDB 1h1d: Catechol O-Methyltransferase

Enzymatic activity of Catechol O-Methyltransferase

All present enzymatic activity of Catechol O-Methyltransferase:
2.1.1.6;

Protein crystallography data

The structure of Catechol O-Methyltransferase, PDB code: 1h1d was solved by M.Archer, M.L.Rodrigues, P.M.Matias, M.J.Bonifacio, D.A.Learmonth, P.Soares-Da-Silva, M.A.Carrondo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.80 / 2.00
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 51.490, 51.490, 168.290, 90.00, 90.00, 120.00
R / Rfree (%) 17.4 / 19.8

Other elements in 1h1d:

The structure of Catechol O-Methyltransferase also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Catechol O-Methyltransferase (pdb code 1h1d). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Catechol O-Methyltransferase, PDB code: 1h1d:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in 1h1d

Go back to Fluorine Binding Sites List in 1h1d
Fluorine binding site 1 out of 3 in the Catechol O-Methyltransferase


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Catechol O-Methyltransferase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F335

b:66.7
occ:1.00
F37 A:BIA335 0.0 66.7 1.0
C33 A:BIA335 1.4 64.5 1.0
F38 A:BIA335 2.1 65.3 1.0
F39 A:BIA335 2.1 67.1 1.0
C24 A:BIA335 2.3 62.6 1.0
C37 A:BIA335 2.8 60.6 1.0
C26 A:BIA335 3.5 59.3 1.0
C10 A:BIA335 4.1 58.5 1.0
C31 A:BIA335 4.7 55.8 1.0
C4 A:BIA335 4.9 57.0 1.0

Fluorine binding site 2 out of 3 in 1h1d

Go back to Fluorine Binding Sites List in 1h1d
Fluorine binding site 2 out of 3 in the Catechol O-Methyltransferase


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Catechol O-Methyltransferase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F335

b:65.3
occ:1.00
F38 A:BIA335 0.0 65.3 1.0
C33 A:BIA335 1.3 64.5 1.0
F37 A:BIA335 2.1 66.7 1.0
F39 A:BIA335 2.1 67.1 1.0
C24 A:BIA335 2.3 62.6 1.0
C26 A:BIA335 2.7 59.3 1.0
C37 A:BIA335 3.6 60.6 1.0
C31 A:BIA335 4.1 55.8 1.0
C25 A:BIA335 4.7 50.8 1.0
C10 A:BIA335 4.7 58.5 1.0
N2 A:BIA335 4.9 52.6 1.0
C4 A:BIA335 4.9 57.0 1.0

Fluorine binding site 3 out of 3 in 1h1d

Go back to Fluorine Binding Sites List in 1h1d
Fluorine binding site 3 out of 3 in the Catechol O-Methyltransferase


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Catechol O-Methyltransferase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F335

b:67.1
occ:1.00
F39 A:BIA335 0.0 67.1 1.0
C33 A:BIA335 1.2 64.5 1.0
F37 A:BIA335 2.1 66.7 1.0
F38 A:BIA335 2.1 65.3 1.0
C24 A:BIA335 2.2 62.6 1.0
C37 A:BIA335 3.0 60.6 1.0
C26 A:BIA335 3.2 59.3 1.0
C10 A:BIA335 4.3 58.5 1.0
C31 A:BIA335 4.4 55.8 1.0
CE A:MET201 4.9 47.0 1.0
C4 A:BIA335 4.9 57.0 1.0

Reference:

M.J.Bonifacio, M.Archer, M.L.Rodrigues, P.M.Matias, D.A.Learmonth, M.A.Carrondo, P.Soares-Da-Silva. Kinetics and Crystal Structure of Catechol-O-Methyltransferase Complex with Co-Substrate and A Novel Inhibitor with Potential Therapeutic Application Mol.Pharmacol. V. 62 795 2002.
ISSN: ISSN 0026-895X
PubMed: 12237326
DOI: 10.1124/MOL.62.4.795
Page generated: Sun Dec 13 11:29:55 2020

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