Iron in PDB 3kcy: Factor Inhibiting Hif-1 Alpha in Complex with 8-Hydroxyquinoline

All present enzymatic activity of Factor Inhibiting Hif-1 Alpha in Complex with 8-Hydroxyquinoline:
1.14.11.16;

The structure of Factor Inhibiting Hif-1 Alpha in Complex with 8-Hydroxyquinoline, PDB code: 3kcy was solved by H.Moon, S.Han, J.Choe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.14 / 2.59
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	86.912, 86.912, 144.559, 90.00, 90.00, 90.00
R / Rfree (%)	25.5 / 33.5

The binding sites of Iron atom in the Factor Inhibiting Hif-1 Alpha in Complex with 8-Hydroxyquinoline (pdb code 3kcy). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Factor Inhibiting Hif-1 Alpha in Complex with 8-Hydroxyquinoline, PDB code: 3kcy:

Iron binding site 1 out of 1 in the Factor Inhibiting Hif-1 Alpha in Complex with 8-Hydroxyquinoline


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Factor Inhibiting Hif-1 Alpha in Complex with 8-Hydroxyquinoline within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1350 b:77.9 occ:1.00 OAA A:HQY1 2.0 0.5 1.0 NE2 A:HIS199 2.2 47.6 1.0 NE2 A:HIS279 2.2 45.6 1.0 OD2 A:ASP201 2.3 52.4 1.0 NAH A:HQY1 2.4 99.8 1.0 CAJ A:HQY1 2.8 0.7 1.0 CAM A:HQY1 3.0 0.4 1.0 CE1 A:HIS199 3.0 48.7 1.0 CE1 A:HIS279 3.1 43.3 1.0 CG A:ASP201 3.2 48.1 1.0 CD2 A:HIS199 3.3 45.7 1.0 OD1 A:ASP201 3.3 52.2 1.0 CD2 A:HIS279 3.3 42.5 1.0 CAE A:HQY1 3.5 0.3 1.0 CZ2 A:TRP296 4.0 68.3 1.0 CAK A:HQY1 4.1 0.3 1.0 ND1 A:HIS199 4.2 48.3 1.0 ND1 A:HIS279 4.3 42.7 1.0 CG A:HIS199 4.3 45.2 1.0 CAL A:HQY1 4.3 99.7 1.0 CG A:HIS279 4.4 41.6 1.0 CB A:ASP201 4.6 46.1 1.0 CAD A:HQY1 4.7 0.3 1.0 CH2 A:TRP296 4.9 68.0 1.0 CE2 A:TRP296 4.9 68.6 1.0

H.Moon, S.Han, H.Park, J.Choe. Crystal Structures of Human Fih-1 in Complex with Quinol Family Inhibitors Mol.Cells V. 29 471 2010.
ISSN: ISSN 1016-8478
PubMed: 20396966
DOI: 10.1007/S10059-010-0058-3