Iodine in PDB 1n7j: The Structure of Phenylethanolamine N-Methyltransferase in Complex with S-Adenosylhomocysteine and An Iodinated Inhibitor

All present enzymatic activity of The Structure of Phenylethanolamine N-Methyltransferase in Complex with S-Adenosylhomocysteine and An Iodinated Inhibitor:
2.1.1.28;

The structure of The Structure of Phenylethanolamine N-Methyltransferase in Complex with S-Adenosylhomocysteine and An Iodinated Inhibitor, PDB code: 1n7j was solved by F.M.Mcmillan, J.Archbold, M.J.Mcleish, J.M.Caine, K.R.Criscione, G.L.Grunewald, J.L.Martin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.39 / 2.70
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	94.740, 94.740, 186.900, 90.00, 90.00, 90.00
R / Rfree (%)	23.2 / 26.8

The binding sites of Iodine atom in the The Structure of Phenylethanolamine N-Methyltransferase in Complex with S-Adenosylhomocysteine and An Iodinated Inhibitor (pdb code 1n7j). This binding sites where shown within 5.0 Angstroms radius around Iodine atom.
In total 2 binding sites of Iodine where determined in the The Structure of Phenylethanolamine N-Methyltransferase in Complex with S-Adenosylhomocysteine and An Iodinated Inhibitor, PDB code: 1n7j:
Jump to Iodine binding site number: 1; 2;

Iodine binding site 1 out of 2 in the The Structure of Phenylethanolamine N-Methyltransferase in Complex with S-Adenosylhomocysteine and An Iodinated Inhibitor


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 1 of The Structure of Phenylethanolamine N-Methyltransferase in Complex with S-Adenosylhomocysteine and An Iodinated Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:I3003 b:84.3 occ:1.00 I A:IDI3003 0.0 84.3 1.0 C6 A:IDI3003 2.0 77.7 1.0 C7 A:IDI3003 3.0 76.2 1.0 CE A:MET258 3.0 23.4 1.0 C5 A:IDI3003 3.0 75.3 1.0 CG1 A:VAL53 3.8 35.3 1.0 NH1 A:ARG44 4.0 41.8 1.0 CB A:VAL53 4.1 35.1 1.0 CG2 A:VAL53 4.2 35.0 1.0 C8 A:IDI3003 4.3 73.3 1.0 C4 A:IDI3003 4.3 73.2 1.0 SD A:MET258 4.3 35.2 1.0 CG2 A:VAL272 4.3 35.6 1.0 CD A:ARG44 4.4 40.9 1.0 CZ A:PHE182 4.5 38.3 1.0 CZ A:ARG44 4.6 43.0 1.0 NZ A:LYS57 4.6 25.2 1.0 CE A:LYS57 4.7 25.1 1.0 NE A:ARG44 4.7 42.9 1.0 CE2 A:PHE182 4.8 37.5 1.0 C9 A:IDI3003 4.8 73.2 1.0

Iodine binding site 2 out of 2 in the The Structure of Phenylethanolamine N-Methyltransferase in Complex with S-Adenosylhomocysteine and An Iodinated Inhibitor


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 2 of The Structure of Phenylethanolamine N-Methyltransferase in Complex with S-Adenosylhomocysteine and An Iodinated Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:I3002 b:1.0 occ:1.00 I B:IDI3002 0.0 1.0 1.0 C6 B:IDI3002 2.0 0.9 1.0 C7 B:IDI3002 3.0 0.4 1.0 C5 B:IDI3002 3.0 1.0 1.0 CE B:MET758 3.0 19.1 1.0 SD B:MET758 3.9 33.9 1.0 CG1 B:VAL553 4.0 38.8 1.0 NH1 B:ARG544 4.1 38.6 1.0 CZ B:PHE682 4.2 21.7 1.0 CG2 B:VAL772 4.2 22.5 1.0 C4 B:IDI3002 4.3 0.8 1.0 C8 B:IDI3002 4.3 0.3 1.0 NZ B:LYS557 4.4 21.7 1.0 CB B:VAL553 4.5 39.2 1.0 CD B:ARG544 4.6 45.5 1.0 CG2 B:VAL553 4.6 39.5 1.0 CE1 B:PHE682 4.7 21.7 1.0 CZ B:ARG544 4.7 42.4 1.0 CE2 B:PHE682 4.8 21.9 1.0 C9 B:IDI3002 4.8 0.2 1.0 CE B:LYS557 4.8 20.7 1.0 OD1 B:ASN539 4.8 46.0 1.0 NE B:ARG544 4.9 43.5 1.0

F.M.Mcmillan, J.Archbold, M.J.Mcleish, J.M.Caine, K.R.Criscione, G.L.Grunewald, J.L.Martin. Molecular Recognition of Sub-Micromolar Inhibitors By the Epinephrine-Synthesizing Enzyme Phenylethanolamine N-Methyltransferase. J.Med.Chem. V. 47 37 2004.
ISSN: ISSN 0022-2623
PubMed: 14695818
DOI: 10.1021/JM0205752