Fluorine in PDB 1h1d: Catechol O-Methyltransferase

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

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

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

Magnesium

(Mg)

1 atom

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 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 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 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

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