Iron in PDB 4z1v: Structure of Factor Inhibiting Hif (Fih) in Complex with Fe, No, and Nog

All present enzymatic activity of Structure of Factor Inhibiting Hif (Fih) in Complex with Fe, No, and Nog:
1.14.11.30;

The structure of Structure of Factor Inhibiting Hif (Fih) in Complex with Fe, No, and Nog, PDB code: 4z1v was solved by C.Y.Taabazuing, S.C.Garman, M.J.Knapp, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	74.74 / 2.10
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	86.650, 86.650, 147.730, 90.00, 90.00, 90.00
R / Rfree (%)	19 / 24

The binding sites of Iron atom in the Structure of Factor Inhibiting Hif (Fih) in Complex with Fe, No, and Nog (pdb code 4z1v). 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 Structure of Factor Inhibiting Hif (Fih) in Complex with Fe, No, and Nog, PDB code: 4z1v:

Iron binding site 1 out of 1 in the Structure of Factor Inhibiting Hif (Fih) in Complex with Fe, No, and Nog


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Factor Inhibiting Hif (Fih) in Complex with Fe, No, and Nog within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe604 b:36.6 occ:1.00 N A:NO602 1.8 50.4 1.0 NE2 A:HIS279 2.0 37.3 1.0 O2 A:OGA601 2.0 40.3 1.0 NE2 A:HIS199 2.0 38.4 1.0 OD2 A:ASP201 2.0 30.7 1.0 O2' A:OGA601 2.1 36.8 1.0 C1 A:OGA601 2.8 37.1 1.0 O A:NO602 2.8 67.1 1.0 C2 A:OGA601 2.8 38.6 1.0 CE1 A:HIS279 2.9 36.8 1.0 CE1 A:HIS199 3.0 39.8 1.0 CD2 A:HIS279 3.1 38.2 1.0 CD2 A:HIS199 3.1 36.5 1.0 CG A:ASP201 3.1 37.5 1.0 OD1 A:ASP201 3.5 37.4 1.0 O1 A:OGA601 4.0 41.2 1.0 O A:HOH764 4.1 38.0 1.0 ND1 A:HIS279 4.1 40.6 1.0 ND1 A:HIS199 4.1 37.0 1.0 N1 A:OGA601 4.1 36.4 1.0 CG A:HIS279 4.2 39.5 1.0 CG A:HIS199 4.2 34.7 1.0 CZ2 A:TRP296 4.3 51.4 1.0 CB A:ASP201 4.5 36.2 1.0 C2 A:PEG603 4.5 66.3 1.0 O2 A:PEG603 4.6 72.7 1.0 C4 A:OGA601 4.9 36.6 1.0

C.Y.Taabazuing, J.Fermann, S.Garman, M.J.Knapp. Substrate Promotes Productive Gas Binding in the Alpha-Ketoglutarate-Dependent Oxygenase Fih. Biochemistry V. 55 277 2016.
ISSN: ISSN 0006-2960
PubMed: 26727884
DOI: 10.1021/ACS.BIOCHEM.5B01003