Iodine in PDB 2ohn: X-Ray Crystal Structure of Beta Secretase Complexed with 4-(4- Fluorobenzyl)Piperidine

All present enzymatic activity of X-Ray Crystal Structure of Beta Secretase Complexed with 4-(4- Fluorobenzyl)Piperidine:
3.4.23.46;

The structure of X-Ray Crystal Structure of Beta Secretase Complexed with 4-(4- Fluorobenzyl)Piperidine, PDB code: 2ohn was solved by S.Patel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.79 / 2.15
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	102.388, 102.388, 170.232, 90.00, 90.00, 120.00
R / Rfree (%)	22.8 / 28.5

The structure of X-Ray Crystal Structure of Beta Secretase Complexed with 4-(4- Fluorobenzyl)Piperidine also contains other interesting chemical elements:

Fluorine

(F)

1 atom

The binding sites of Iodine atom in the X-Ray Crystal Structure of Beta Secretase Complexed with 4-(4- Fluorobenzyl)Piperidine (pdb code 2ohn). This binding sites where shown within 5.0 Angstroms radius around Iodine atom.
In total 3 binding sites of Iodine where determined in the X-Ray Crystal Structure of Beta Secretase Complexed with 4-(4- Fluorobenzyl)Piperidine, PDB code: 2ohn:
Jump to Iodine binding site number: 1; 2; 3;

Iodine binding site 1 out of 3 in the X-Ray Crystal Structure of Beta Secretase Complexed with 4-(4- Fluorobenzyl)Piperidine


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 1 of X-Ray Crystal Structure of Beta Secretase Complexed with 4-(4- Fluorobenzyl)Piperidine within 5.0Å range: probe atom residue distance (Å) B Occ A:I401 b:25.1 occ:0.50 O A:HOH590 3.1 34.8 1.0 OG A:SER105 3.5 28.2 1.0 O A:HOH591 3.5 28.0 1.0 CA A:GLU104 3.7 31.1 1.0 N A:SER105 3.7 26.5 1.0 C A:GLU104 3.8 28.8 1.0 N A:GLU104 3.8 30.6 1.0 C A:THR103 3.9 31.5 1.0 O A:THR103 4.1 28.2 1.0 ND1 A:HIS45 4.1 24.3 1.0 CB A:HIS45 4.1 23.9 1.0 CB A:SER105 4.2 27.6 1.0 CE2 A:PHE109 4.2 27.4 1.0 CG2 A:ILE102 4.4 19.7 1.0 O A:ILE102 4.5 22.1 1.0 O A:GLU104 4.5 26.3 1.0 CG A:HIS45 4.6 21.1 1.0 CA A:SER105 4.6 28.7 1.0 CA A:THR103 4.7 28.4 1.0 CD2 A:PHE109 4.8 23.3 1.0 C A:ILE102 4.8 24.3 1.0 O A:HOH613 4.8 36.1 1.0 N A:THR103 4.8 25.5 1.0 CB A:ALA43 5.0 21.8 1.0

Iodine binding site 2 out of 3 in the X-Ray Crystal Structure of Beta Secretase Complexed with 4-(4- Fluorobenzyl)Piperidine


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 2 of X-Ray Crystal Structure of Beta Secretase Complexed with 4-(4- Fluorobenzyl)Piperidine within 5.0Å range: probe atom residue distance (Å) B Occ A:I402 b:59.4 occ:0.25 O A:ARG96 3.6 32.1 1.0 OE1 A:GLU134 4.1 40.6 1.0 NE2 A:GLN143 4.1 30.4 1.0 O A:HOH496 4.2 34.5 1.0 OG A:SER139 4.4 26.8 1.0 C A:ARG96 4.4 33.9 1.0 ND2 A:ASN98 4.5 31.7 1.0 O A:HOH439 4.5 35.2 1.0 CG A:ARG96 4.6 37.9 1.0 O A:HOH574 4.7 42.2 1.0 CG2 A:THR82 4.7 24.9 1.0 CA A:ALA97 4.8 31.7 1.0 N A:ASN98 4.8 28.8 1.0 O A:HOH597 4.8 26.8 1.0 OD1 A:ASN98 4.9 35.0 1.0 CG A:ASN98 4.9 38.0 1.0 N A:ALA97 4.9 32.0 1.0 C A:ALA97 4.9 28.8 1.0 CD A:GLU134 5.0 40.9 1.0

Iodine binding site 3 out of 3 in the X-Ray Crystal Structure of Beta Secretase Complexed with 4-(4- Fluorobenzyl)Piperidine


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 3 of X-Ray Crystal Structure of Beta Secretase Complexed with 4-(4- Fluorobenzyl)Piperidine within 5.0Å range: probe atom residue distance (Å) B Occ A:I403 b:33.8 occ:0.25 N A:LYS107 3.5 27.1 1.0 O A:HOH614 3.6 40.2 1.0 O A:HOH593 3.7 26.6 1.0 CE1 A:HIS45 3.8 23.2 1.0 CA A:ASP106 4.3 28.9 1.0 CA A:LYS107 4.3 27.3 1.0 C A:ASP106 4.4 29.5 1.0 NE2 A:HIS45 4.4 27.5 1.0 O A:SER105 4.6 32.6 1.0 CE2 A:PHE47 4.6 40.5 1.0 ND1 A:HIS45 5.0 24.3 1.0 CG A:LYS107 5.0 33.3 1.0 OD1 A:ASP106 5.0 27.6 0.5 N A:ASP106 5.0 30.9 1.0

C.W.Murray, O.Callaghan, G.Chessari, A.Cleasby, M.Congreve, M.Frederickson, M.J.Hartshorn, R.Mcmenamin, S.Patel, N.Wallis. Application of Fragment Screening By X-Ray Crystallography to Beta-Secretase. J.Med.Chem. V. 50 1116 2007.
ISSN: ISSN 0022-2623
PubMed: 17315856
DOI: 10.1021/JM0611962