Fluorine in PDB 3lj1: IRE1 Complexed with CDK1/2 Inhibitor III

All present enzymatic activity of IRE1 Complexed with CDK1/2 Inhibitor III:
2.7.11.1;

The structure of IRE1 Complexed with CDK1/2 Inhibitor III, PDB code: 3lj1 was solved by K.P.K.Lee, F.Sicheri, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	51.26 / 3.33
Space group	P 32 1 2
Cell size a, b, c (Å), α, β, γ (°)	125.550, 125.550, 174.390, 90.00, 90.00, 120.00
R / Rfree (%)	26.3 / 28.4

The binding sites of Fluorine atom in the IRE1 Complexed with CDK1/2 Inhibitor III (pdb code 3lj1). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the IRE1 Complexed with CDK1/2 Inhibitor III, PDB code: 3lj1:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in the IRE1 Complexed with CDK1/2 Inhibitor III


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of IRE1 Complexed with CDK1/2 Inhibitor III within 5.0Å range: probe atom residue distance (Å) B Occ A:F1 b:67.3 occ:1.00 FAF A:DKI1 0.0 67.3 1.0 CAU A:DKI1 1.4 66.1 1.0 CAI A:DKI1 2.4 66.6 1.0 CAZ A:DKI1 2.4 64.4 1.0 NAQ A:DKI1 2.7 61.5 1.0 O A:LEU680 3.2 63.3 1.0 CA A:GLY681 3.4 62.5 1.0 CAH A:DKI1 3.7 66.3 1.0 C A:LEU680 3.7 63.1 1.0 CAV A:DKI1 3.8 65.4 1.0 N A:GLY681 3.8 62.7 1.0 CAS A:DKI1 4.0 58.5 1.0 NAP A:DKI1 4.1 56.6 1.0 ND2 A:ASN751 4.1 60.0 1.0 CAJ A:DKI1 4.2 65.9 1.0 CAL A:DKI1 4.2 55.2 1.0 CAN A:DKI1 4.4 55.3 1.0 C A:GLY681 4.4 62.4 1.0 NBA A:DKI1 4.5 57.0 1.0 CB A:LEU680 4.7 61.6 1.0 CA A:LEU680 4.8 63.8 1.0 O A:GLN801 4.9 54.3 1.0 FAG A:DKI1 4.9 66.5 1.0 CD2 A:LEU804 5.0 52.1 1.0

Fluorine binding site 2 out of 4 in the IRE1 Complexed with CDK1/2 Inhibitor III


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of IRE1 Complexed with CDK1/2 Inhibitor III within 5.0Å range: probe atom residue distance (Å) B Occ A:F1 b:66.5 occ:1.00 FAG A:DKI1 0.0 66.5 1.0 CAV A:DKI1 1.3 65.4 1.0 SAE A:DKI1 2.3 56.6 1.0 CAJ A:DKI1 2.4 65.9 1.0 CAZ A:DKI1 2.5 64.4 1.0 NAQ A:DKI1 3.0 61.5 1.0 CAS A:DKI1 3.0 58.5 1.0 OG A:SER827 3.5 50.7 1.0 CAH A:DKI1 3.6 66.3 1.0 CAU A:DKI1 3.8 66.1 1.0 CAI A:DKI1 4.2 66.6 1.0 NBA A:DKI1 4.4 57.0 1.0 CB A:ASP828 4.4 53.0 1.0 CG2 A:VAL689 4.6 56.7 1.0 CB A:SER827 4.6 50.3 1.0 N A:ASP828 4.7 51.5 1.0 CD1 A:LEU804 4.8 51.1 1.0 CA A:ASP828 4.9 52.5 1.0 O A:GLN801 4.9 54.3 1.0 OD2 A:ASP828 4.9 55.9 1.0 FAF A:DKI1 4.9 67.3 1.0 CG A:ASP828 4.9 54.3 1.0

Fluorine binding site 3 out of 4 in the IRE1 Complexed with CDK1/2 Inhibitor III


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of IRE1 Complexed with CDK1/2 Inhibitor III within 5.0Å range: probe atom residue distance (Å) B Occ B:F1 b:48.8 occ:1.00 FAF B:DKI1 0.0 48.8 1.0 CAU B:DKI1 1.3 48.0 1.0 CAI B:DKI1 2.4 48.0 1.0 CAZ B:DKI1 2.5 47.5 1.0 OG B:SER827 2.8 48.9 1.0 NAQ B:DKI1 2.9 46.8 1.0 O B:GLN801 3.3 49.2 1.0 CAS B:DKI1 3.3 45.4 1.0 SAE B:DKI1 3.4 45.0 1.0 CAH B:DKI1 3.7 48.0 1.0 CAV B:DKI1 3.8 47.7 1.0 CA B:ASN802 3.8 45.5 1.0 OD1 B:ASN802 4.0 47.5 1.0 CD2 B:LEU804 4.1 50.4 1.0 CD1 B:LEU804 4.2 51.0 1.0 CB B:SER827 4.2 49.0 1.0 CAJ B:DKI1 4.2 47.8 1.0 CG B:LEU804 4.3 49.6 1.0 CB B:ASP828 4.3 48.6 1.0 C B:GLN801 4.3 47.8 1.0 C B:ASN802 4.4 44.7 1.0 NBA B:DKI1 4.5 43.8 1.0 N B:ASN802 4.6 46.1 1.0 O B:ASN802 4.6 44.5 1.0 N B:ASP828 4.6 48.8 1.0 CG B:ASN802 4.6 45.6 1.0 CB B:ASN802 4.7 44.7 1.0 C B:SER827 4.7 47.3 1.0 FAG B:DKI1 4.9 48.2 1.0 OD2 B:ASP828 5.0 50.5 1.0 CA B:ASP828 5.0 49.0 1.0

Fluorine binding site 4 out of 4 in the IRE1 Complexed with CDK1/2 Inhibitor III


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of IRE1 Complexed with CDK1/2 Inhibitor III within 5.0Å range: probe atom residue distance (Å) B Occ B:F1 b:48.2 occ:1.00 FAG B:DKI1 0.0 48.2 1.0 CAV B:DKI1 1.3 47.7 1.0 CAJ B:DKI1 2.4 47.8 1.0 CAZ B:DKI1 2.4 47.5 1.0 NAQ B:DKI1 2.8 46.8 1.0 CA B:GLY681 3.0 61.4 1.0 N B:GLY681 3.1 63.1 1.0 CAS B:DKI1 3.4 45.4 1.0 C B:GLY681 3.4 61.2 1.0 CB B:VAL689 3.4 60.5 1.0 C B:LEU680 3.5 63.6 1.0 CG2 B:VAL689 3.6 58.2 1.0 O B:GLY681 3.6 61.8 1.0 CAH B:DKI1 3.7 48.0 1.0 CAU B:DKI1 3.8 48.0 1.0 O B:LEU680 3.8 62.8 1.0 CG1 B:VAL689 3.9 60.8 1.0 NAP B:DKI1 4.1 42.9 1.0 NBA B:DKI1 4.1 43.8 1.0 CB B:LEU680 4.1 64.2 1.0 SAE B:DKI1 4.2 45.0 1.0 CAI B:DKI1 4.2 48.0 1.0 N B:TYR682 4.3 60.6 1.0 CA B:LEU680 4.5 65.7 1.0 CA B:VAL689 4.8 63.0 1.0 CAL B:DKI1 4.9 42.2 1.0 FAF B:DKI1 4.9 48.8 1.0 O B:VAL689 5.0 66.1 1.0 O B:TYR682 5.0 56.4 1.0

R.L.Wiseman, Y.Zhang, K.P.Lee, H.P.Harding, C.M.Haynes, J.Price, F.Sicheri, D.Ron. Flavonol Activation Defines An Unanticipated Ligand-Binding Site in the Kinase-Rnase Domain of IRE1. Mol.Cell V. 38 291 2010.
ISSN: ISSN 1097-2765
PubMed: 20417606
DOI: 10.1016/J.MOLCEL.2010.04.001