Fluorine in PDB 3zkn: BACE2 Fab Inhibitor Complex

All present enzymatic activity of BACE2 Fab Inhibitor Complex:
3.4.23.45;

The structure of BACE2 Fab Inhibitor Complex, PDB code: 3zkn was solved by D.W.Banner, A.Kuglstatter, J.Benz, M.Stihle, A.Ruf, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.75 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	81.929, 68.145, 160.855, 90.00, 92.51, 90.00
R / Rfree (%)	20.318 / 25.141

The binding sites of Fluorine atom in the BACE2 Fab Inhibitor Complex (pdb code 3zkn). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 6 binding sites of Fluorine where determined in the BACE2 Fab Inhibitor Complex, PDB code: 3zkn:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6;

Fluorine binding site 1 out of 6 in the BACE2 Fab Inhibitor Complex


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of BACE2 Fab Inhibitor Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:F1398 b:95.7 occ:1.00 F30 A:WZV1398 0.0 95.7 1.0 C28 A:WZV1398 1.3 96.5 1.0 F29 A:WZV1398 2.2 99.2 1.0 F31 A:WZV1398 2.2 95.7 1.0 C27 A:WZV1398 2.3 89.4 1.0 O26 A:WZV1398 2.8 78.3 1.0 C18 A:WZV1398 4.2 66.2 1.0 OE1 A:GLN89 4.4 39.2 0.5 OD1 A:ASN123 4.4 40.2 1.0 ND2 A:ASN123 4.5 34.6 1.0 CG A:ASN123 4.6 36.1 1.0 C23 A:WZV1398 5.0 60.5 1.0

Fluorine binding site 2 out of 6 in the BACE2 Fab Inhibitor Complex


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of BACE2 Fab Inhibitor Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:F1398 b:95.7 occ:1.00 F31 A:WZV1398 0.0 95.7 1.0 C28 A:WZV1398 1.3 96.5 1.0 F29 A:WZV1398 2.2 99.2 1.0 F30 A:WZV1398 2.2 95.7 1.0 C27 A:WZV1398 2.3 89.4 1.0 OE1 A:GLN89 3.3 39.2 0.5 O26 A:WZV1398 3.6 78.3 1.0 CD A:GLN89 4.4 38.2 0.5 C18 A:WZV1398 4.7 66.2 1.0 NE2 A:GLN89 4.9 35.9 0.5

Fluorine binding site 3 out of 6 in the BACE2 Fab Inhibitor Complex


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of BACE2 Fab Inhibitor Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:F1398 b:99.2 occ:1.00 F29 A:WZV1398 0.0 99.2 1.0 C28 A:WZV1398 1.3 96.5 1.0 F30 A:WZV1398 2.2 95.7 1.0 F31 A:WZV1398 2.2 95.7 1.0 C27 A:WZV1398 2.3 89.4 1.0 OE1 A:GLN89 2.4 39.2 0.5 O26 A:WZV1398 2.8 78.3 1.0 CD A:GLN89 3.3 38.2 0.5 CB A:GLN89 3.8 38.9 1.0 C18 A:WZV1398 3.9 66.2 1.0 CG A:GLN89 4.0 37.9 0.5 C23 A:WZV1398 4.0 60.5 1.0 NE2 A:GLN89 4.2 35.9 0.5 ND2 A:ASN123 4.3 34.6 1.0 CG A:ASN123 4.8 36.1 1.0

Fluorine binding site 4 out of 6 in the BACE2 Fab Inhibitor Complex


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of BACE2 Fab Inhibitor Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:F1398 b:72.4 occ:1.00 F30 B:WZV1398 0.0 72.4 1.0 C28 B:WZV1398 1.3 74.7 1.0 F29 B:WZV1398 2.2 74.4 1.0 F31 B:WZV1398 2.2 74.2 1.0 C27 B:WZV1398 2.3 69.8 1.0 O26 B:WZV1398 3.2 62.7 1.0 OD1 B:ASN123 4.0 32.2 1.0 C18 B:WZV1398 4.3 52.2 1.0 CG B:ASN123 4.5 29.6 1.0 ND2 B:ASN123 4.5 30.0 1.0 C19 B:WZV1398 4.6 48.7 1.0 CD1 B:LEU126 4.9 39.4 1.0

Fluorine binding site 5 out of 6 in the BACE2 Fab Inhibitor Complex


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of BACE2 Fab Inhibitor Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:F1398 b:74.2 occ:1.00 F31 B:WZV1398 0.0 74.2 1.0 C28 B:WZV1398 1.3 74.7 1.0 F29 B:WZV1398 2.2 74.4 1.0 F30 B:WZV1398 2.2 72.4 1.0 C27 B:WZV1398 2.3 69.8 1.0 O26 B:WZV1398 3.5 62.7 1.0 OE1 B:GLN89 3.5 63.8 1.0 CD B:GLN89 4.6 62.7 1.0 C18 B:WZV1398 4.8 52.2 1.0

Fluorine binding site 6 out of 6 in the BACE2 Fab Inhibitor Complex


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of BACE2 Fab Inhibitor Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:F1398 b:74.4 occ:1.00 F29 B:WZV1398 0.0 74.4 1.0 C28 B:WZV1398 1.3 74.7 1.0 F30 B:WZV1398 2.2 72.4 1.0 F31 B:WZV1398 2.2 74.2 1.0 C27 B:WZV1398 2.4 69.8 1.0 O26 B:WZV1398 2.6 62.7 1.0 ND2 B:ASN123 3.3 30.0 1.0 OE1 B:GLN89 3.3 63.8 1.0 CG B:ASN123 3.9 29.6 1.0 OD1 B:ASN123 4.0 32.2 1.0 C18 B:WZV1398 4.0 52.2 1.0 CD B:GLN89 4.3 62.7 1.0 CB B:GLN89 4.7 49.8 1.0 C23 B:WZV1398 4.8 49.4 1.0 C19 B:WZV1398 4.9 48.7 1.0 CG B:GLN89 5.0 55.7 1.0

D.W.Banner, B.Gsell, J.Benz, J.Bertschinger, D.Burger, S.Brack, S.Cuppuleri, M.Debulpaep, A.Gast, D.Grabulovski, M.Hennig, H.Hilpert, W.Huber, A.Kuglstatter, E.Kusznir, T.Laeremans, H.Matile, C.Miscenic, A.Rufer, D.Schlatter, J.Steyeart, M.Stihle, R.Thoma, M.Weber, A.Ruf. Mapping the Conformational Space Accessible to BACE2 Using Surface Mutants and Co-Crystals with Fab-Fragments, Fynomers, and Xaperones Acta Crystallogr.,Sect.D V. 69 1124 2013.
ISSN: ISSN 0907-4449
PubMed: 23695257
DOI: 10.1107/S0907444913006574