Fluorine in PDB 4ogh: Crystal Structure of T877A-Ar-Lbd

The structure of Crystal Structure of T877A-Ar-Lbd, PDB code: 4ogh was solved by J.S.Liu, C.L.Hsu, W.G.Wu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.98
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.007, 65.759, 70.736, 90.00, 90.00, 90.00
R / Rfree (%)	16.2 / 24

The binding sites of Fluorine atom in the Crystal Structure of T877A-Ar-Lbd (pdb code 4ogh). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Crystal Structure of T877A-Ar-Lbd, PDB code: 4ogh:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of T877A-Ar-Lbd


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of T877A-Ar-Lbd within 5.0Å range: probe atom residue distance (Å) B Occ A:F1001 b:37.2 occ:1.00 F1 A:HFT1001 0.0 37.2 1.0 C7 A:HFT1001 1.3 42.1 1.0 F3 A:HFT1001 2.2 40.5 1.0 F2 A:HFT1001 2.2 42.8 1.0 C3 A:HFT1001 2.3 41.4 1.0 C2 A:HFT1001 2.6 41.4 1.0 CD1 A:LEU873 3.3 32.4 1.0 SD A:MET787 3.7 43.5 1.0 C4 A:HFT1001 3.7 44.7 1.0 O10 A:HFT1001 3.8 45.2 1.0 CD2 A:LEU873 3.8 32.0 1.0 C1 A:HFT1001 4.0 42.9 1.0 CE2 A:PHE764 4.0 30.8 1.0 CG2 A:VAL746 4.1 26.4 1.0 SD A:MET742 4.1 33.2 1.0 CG A:LEU873 4.1 32.2 1.0 N1 A:HFT1001 4.4 50.0 1.0 O1 A:HFT1001 4.4 58.1 1.0 CE A:MET787 4.5 38.1 1.0 C10 A:HFT1001 4.6 43.1 1.0 N9 A:HFT1001 4.7 45.5 1.0 C5 A:HFT1001 4.8 44.4 1.0 CD2 A:PHE764 4.8 30.2 1.0 C6 A:HFT1001 4.9 42.5 1.0 CZ A:PHE764 4.9 29.5 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of T877A-Ar-Lbd


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of T877A-Ar-Lbd within 5.0Å range: probe atom residue distance (Å) B Occ A:F1001 b:42.8 occ:1.00 F2 A:HFT1001 0.0 42.8 1.0 C7 A:HFT1001 1.4 42.1 1.0 F3 A:HFT1001 2.1 40.5 1.0 F1 A:HFT1001 2.2 37.2 1.0 C3 A:HFT1001 2.4 41.4 1.0 O1 A:HFT1001 2.7 58.1 1.0 C4 A:HFT1001 3.2 44.7 1.0 N A:VAL746 3.2 26.7 1.0 N1 A:HFT1001 3.3 50.0 1.0 C A:MET745 3.4 29.4 1.0 CG2 A:VAL746 3.4 26.4 1.0 C2 A:HFT1001 3.4 41.4 1.0 CA A:VAL746 3.4 26.4 1.0 CB A:MET745 3.4 30.2 1.0 O A:MET745 3.7 30.0 1.0 O A:MET742 3.9 27.5 1.0 CA A:MET745 4.0 28.4 1.0 CB A:VAL746 4.0 25.9 1.0 CE A:MET745 4.2 33.8 1.0 SD A:MET742 4.4 33.2 1.0 C5 A:HFT1001 4.5 44.4 1.0 CB A:MET749 4.5 34.3 1.0 CD1 A:LEU873 4.6 32.4 1.0 O2 A:HFT1001 4.6 50.6 1.0 C1 A:HFT1001 4.6 42.9 1.0 SD A:MET787 4.7 43.5 1.0 CG A:MET745 4.7 32.0 1.0 C A:VAL746 4.7 27.4 1.0 SD A:MET745 4.9 32.8 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of T877A-Ar-Lbd


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of T877A-Ar-Lbd within 5.0Å range: probe atom residue distance (Å) B Occ A:F1001 b:40.5 occ:1.00 F3 A:HFT1001 0.0 40.5 1.0 C7 A:HFT1001 1.3 42.1 1.0 F2 A:HFT1001 2.1 42.8 1.0 F1 A:HFT1001 2.2 37.2 1.0 C3 A:HFT1001 2.3 41.4 1.0 C4 A:HFT1001 3.0 44.7 1.0 N1 A:HFT1001 3.0 50.0 1.0 O1 A:HFT1001 3.0 58.1 1.0 CE2 A:PHE764 3.0 30.8 1.0 CE A:MET749 3.4 34.4 1.0 CD2 A:PHE764 3.4 30.2 1.0 C2 A:HFT1001 3.4 41.4 1.0 CG A:MET749 3.7 36.2 1.0 SD A:MET787 3.7 43.5 1.0 CB A:MET749 3.8 34.3 1.0 O2 A:HFT1001 3.8 50.6 1.0 CZ A:PHE764 4.2 29.5 1.0 C5 A:HFT1001 4.3 44.4 1.0 SD A:MET749 4.4 36.9 1.0 CA A:VAL746 4.5 26.4 1.0 O A:MET745 4.6 30.0 1.0 C1 A:HFT1001 4.6 42.9 1.0 CG2 A:VAL746 4.7 26.4 1.0 CG A:PHE764 4.7 31.2 1.0 C A:MET745 4.8 29.4 1.0 N A:VAL746 4.8 26.7 1.0 CE A:MET787 4.9 38.1 1.0 C6 A:HFT1001 4.9 42.5 1.0 CD1 A:LEU873 5.0 32.4 1.0

C.L.Hsu, J.S.Liu, P.L.Wu, H.H.Guan, Y.L.Chen, A.C.Lin, H.J.Ting, S.T.Pang, S.D.Yeh, W.L.Ma, C.J.Chen, W.G.Wu, C.Chang. Identification of A New Androgen Receptor (Ar) Co-Regulator BUD31 and Related Peptides to Suppress Wild-Type and Mutated Ar-Mediated Prostate Cancer Growth Via Peptide Screening and X-Ray Structure Analysis. Mol Oncol 2014.
PubMed: 25091737
DOI: 10.1016/J.MOLONC.2014.06.009