Chlorine in PDB 8pdf: FKBP12 in Complex with Protac 6A2

All present enzymatic activity of FKBP12 in Complex with Protac 6A2:
5.2.1.8;

The structure of FKBP12 in Complex with Protac 6A2, PDB code: 8pdf was solved by C.Meyners, M.Walz, T.M.Geiger, F.Hausch, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.79 / 1.20
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	65.993, 36.506, 44.217, 90, 102.19, 90
R / Rfree (%)	15.2 / 17.6

The binding sites of Chlorine atom in the FKBP12 in Complex with Protac 6A2 (pdb code 8pdf). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the FKBP12 in Complex with Protac 6A2, PDB code: 8pdf:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the FKBP12 in Complex with Protac 6A2


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of FKBP12 in Complex with Protac 6A2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl201 b:20.4 occ:1.00 CLAT A:Y5Q201 0.0 20.4 1.0 CAS A:Y5Q201 1.7 16.4 1.0 CAU A:Y5Q201 2.6 15.8 1.0 CAR A:Y5Q201 2.7 15.1 1.0 HAU A:Y5Q201 2.7 15.7 1.0 HB7 A:Y5Q201 2.9 16.7 1.0 HAR A:Y5Q201 2.9 15.1 1.0 HB2 A:ASP37 2.9 19.4 1.0 HG23 A:ILE90 3.3 15.7 1.0 HBJ A:Y5Q201 3.3 16.8 1.0 HD11 A:ILE90 3.4 17.5 1.0 CBJ A:Y5Q201 3.5 16.6 1.0 HBH A:Y5Q201 3.5 17.6 1.0 HD1 A:PHE36 3.6 19.4 1.0 O A:HOH356 3.7 35.9 1.0 OBI A:Y5Q201 3.7 17.2 1.0 CB A:ASP37 3.8 19.3 1.0 O A:PHE36 3.8 21.7 1.0 CG A:ASP37 3.8 21.0 1.0 OD2 A:ASP37 3.8 20.3 1.0 CAV A:Y5Q201 3.9 15.0 1.0 CAQ A:Y5Q201 4.0 14.0 1.0 O A:HOH321 4.0 30.9 1.0 CBH A:Y5Q201 4.1 17.6 1.0 CG2 A:ILE90 4.2 15.8 1.0 HB3 A:ASP37 4.3 19.4 1.0 HG21 A:ILE90 4.3 15.6 1.0 CD1 A:ILE90 4.3 17.8 1.0 OD1 A:ASP37 4.4 22.9 1.0 CAX A:Y5Q201 4.4 15.3 1.0 HD12 A:ILE90 4.5 17.6 1.0 CD1 A:PHE36 4.5 20.0 1.0 HG22 A:ILE90 4.6 15.7 1.0 C A:PHE36 4.7 19.9 1.0 HB2 A:PHE36 4.7 21.0 1.0 HAH A:Y5Q201 4.8 15.8 1.0 HA A:ASP37 4.8 18.5 1.0 CA A:ASP37 4.8 18.6 1.0 HD13 A:ILE90 4.9 17.6 1.0 HB6 A:Y5Q201 4.9 17.6 1.0 HE1 A:PHE36 4.9 19.5 1.0 CBK A:Y5Q201 4.9 16.5 1.0 HBG A:Y5Q201 5.0 18.0 1.0

Chlorine binding site 2 out of 2 in the FKBP12 in Complex with Protac 6A2


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of FKBP12 in Complex with Protac 6A2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl201 b:18.3 occ:1.00 CLAW A:Y5Q201 0.0 18.3 1.0 CAV A:Y5Q201 1.7 15.0 1.0 CAX A:Y5Q201 2.7 15.3 1.0 CAU A:Y5Q201 2.7 15.8 1.0 HAX A:Y5Q201 2.8 15.0 1.0 HBG A:Y5Q201 2.8 18.0 1.0 HAU A:Y5Q201 2.9 15.7 1.0 HB2 A:HIS87 3.3 16.0 1.0 HB3 A:HIS87 3.3 16.1 1.0 HG12 A:ILE91 3.5 18.1 1.0 CG A:HIS87 3.5 17.1 1.0 CB A:HIS87 3.6 15.9 1.0 HG13 A:ILE91 3.6 18.1 1.0 ND1 A:HIS87 3.7 18.6 1.0 CZ A:TYR82 3.7 14.7 1.0 HD1 A:HIS87 3.8 18.7 0.0 HBE A:Y5Q201 3.8 17.9 1.0 CBG A:Y5Q201 3.9 18.3 1.0 OH A:TYR82 3.9 16.0 1.0 CAQ A:Y5Q201 4.0 14.0 1.0 CAS A:Y5Q201 4.0 16.4 1.0 CE1 A:TYR82 4.0 16.5 1.0 CG1 A:ILE91 4.0 18.1 1.0 HD12 A:ILE90 4.0 17.6 1.0 HH A:TYR82 4.0 16.4 0.0 NCQ A:Y5Q201 4.1 15.6 1.0 CE2 A:TYR82 4.1 15.2 1.0 CD2 A:HIS87 4.1 18.9 1.0 HE1 A:TYR82 4.2 15.9 1.0 HB A:ILE90 4.2 15.7 1.0 O A:HOH382 4.3 19.7 1.0 HG23 A:ILE90 4.3 15.7 1.0 CE1 A:HIS87 4.3 18.5 1.0 NCR A:Y5Q201 4.4 14.8 1.0 HB5 A:Y5Q201 4.4 17.9 1.0 HE2 A:TYR82 4.4 15.3 1.0 CAR A:Y5Q201 4.5 15.1 1.0 OBI A:Y5Q201 4.5 17.2 1.0 HD2 A:HIS87 4.5 18.5 1.0 OBF A:Y5Q201 4.5 17.4 1.0 HAF A:Y5Q201 4.5 13.9 1.0 CD1 A:TYR82 4.5 15.9 1.0 NE2 A:HIS87 4.6 19.2 1.0 HD13 A:ILE91 4.6 19.1 1.0 CBE A:Y5Q201 4.6 18.4 1.0 HBH A:Y5Q201 4.6 17.6 1.0 CBH A:Y5Q201 4.6 17.6 1.0 CD2 A:TYR82 4.7 15.1 1.0 HB A:ILE91 4.8 17.2 1.0 HG22 A:ILE90 4.8 15.7 1.0 NBC A:Y5Q201 4.9 15.5 1.0 HE1 A:HIS87 4.9 18.6 1.0 CG A:TYR82 4.9 16.0 1.0 CG2 A:ILE90 4.9 15.8 1.0 CD1 A:ILE91 4.9 19.3 1.0 CD1 A:ILE90 4.9 17.8 1.0 HD11 A:ILE90 5.0 17.5 1.0 CB A:ILE90 5.0 15.3 1.0

T.M.Geiger, M.Walz, C.Meyners, A.Kuehn, J.K.Dreizler, W.O.Sugiarto, E.Maciel, M.Zheng, F.Lermyte, F.Hausch. Discovery of A Potent Protac Enables Targeting of FKBP51'S Scaffolding Functions Angew.Chem.Int.Ed.Engl. 2023.
ISSN: ESSN 1521-3773
DOI: 10.1002/ANIE.202309706