Iron in PDB 4y5t: Structure of FTMOX1 Apo with Metal Iron

All present enzymatic activity of Structure of FTMOX1 Apo with Metal Iron:
1.14.11.38;

The structure of Structure of FTMOX1 Apo with Metal Iron, PDB code: 4y5t was solved by W.Yan, Y.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.91 / 1.95
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	60.445, 45.561, 105.409, 90.00, 99.74, 90.00
R / Rfree (%)	16.4 / 20.4

The structure of Structure of FTMOX1 Apo with Metal Iron also contains other interesting chemical elements:

Cobalt

(Co)

1 atom

The binding sites of Iron atom in the Structure of FTMOX1 Apo with Metal Iron (pdb code 4y5t). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of FTMOX1 Apo with Metal Iron, PDB code: 4y5t:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of FTMOX1 Apo with Metal Iron


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of FTMOX1 Apo with Metal Iron within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:23.6 occ:1.00 OD1 A:ASP135 2.2 15.4 1.0 NE2 A:HIS133 2.4 18.2 1.0 NE2 A:HIS209 2.4 20.4 1.0 O A:HOH774 2.5 26.1 1.0 O A:HOH640 2.5 30.4 1.0 O A:HOH641 2.6 30.3 1.0 CG A:ASP135 3.1 29.3 1.0 CD2 A:HIS209 3.3 18.6 1.0 CD2 A:HIS133 3.3 17.4 1.0 CE1 A:HIS133 3.3 25.5 1.0 OD2 A:ASP135 3.3 26.9 1.0 CE1 A:HIS209 3.3 22.6 1.0 OH A:TYR228 4.3 51.7 1.0 ND1 A:HIS209 4.4 19.4 1.0 ND1 A:HIS133 4.4 22.7 1.0 CG A:HIS209 4.4 15.3 1.0 CG A:HIS133 4.4 15.9 1.0 CB A:ASP135 4.5 18.8 1.0 CA A:ASP135 4.9 21.8 1.0 OE1 A:GLN130 4.9 28.3 1.0 N A:ASP135 5.0 17.9 1.0

Iron binding site 2 out of 2 in the Structure of FTMOX1 Apo with Metal Iron


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of FTMOX1 Apo with Metal Iron within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:26.8 occ:1.00 NE2 B:HIS133 2.3 20.6 1.0 OD1 B:ASP135 2.3 23.0 1.0 NE2 B:HIS209 2.4 28.9 1.0 O B:HOH765 2.4 30.3 1.0 O B:HOH650 2.5 30.0 0.9 O B:HOH649 2.5 37.9 1.0 CG B:ASP135 3.2 37.3 1.0 CD2 B:HIS209 3.2 22.1 1.0 CE1 B:HIS133 3.2 26.0 1.0 OD2 B:ASP135 3.3 29.7 1.0 CD2 B:HIS133 3.4 19.7 1.0 CE1 B:HIS209 3.4 29.1 1.0 O B:HOH754 3.7 46.7 1.0 ND1 B:HIS133 4.3 22.6 1.0 CG B:HIS209 4.4 17.2 1.0 OH B:TYR228 4.4 57.5 1.0 ND1 B:HIS209 4.4 23.1 1.0 CG B:HIS133 4.4 20.1 1.0 O2S B:MES503 4.5 49.9 0.8 CB B:ASP135 4.6 21.4 1.0 OE1 B:GLN130 4.6 32.8 1.0 O3S B:MES503 4.7 42.5 0.8 CA B:ASP135 5.0 26.8 1.0

W.Yan, H.Song, F.Song, Y.Guo, C.H.Wu, A.Sae Her, Y.Pu, S.Wang, N.Naowarojna, A.Weitz, M.P.Hendrich, C.E.Costello, L.Zhang, P.Liu, Y.Jessie Zhang. Endoperoxide Formation By An Alpha-Ketoglutarate-Dependent Mononuclear Non-Haem Iron Enzyme. Nature V. 527 539 2015.
ISSN: ESSN 1476-4687
PubMed: 26524521
DOI: 10.1038/NATURE15519