Iron in PDB 4y5s: Structure of FTMOX1 with A-Ketoglutarate As Co-Substrate

All present enzymatic activity of Structure of FTMOX1 with A-Ketoglutarate As Co-Substrate:
1.14.11.38;

The structure of Structure of FTMOX1 with A-Ketoglutarate As Co-Substrate, PDB code: 4y5s 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)	36.13 / 2.54
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	60.532, 45.659, 105.201, 90.00, 99.98, 90.00
R / Rfree (%)	17.6 / 23.4

The structure of Structure of FTMOX1 with A-Ketoglutarate As Co-Substrate also contains other interesting chemical elements:

Cobalt

(Co)

1 atom

The binding sites of Iron atom in the Structure of FTMOX1 with A-Ketoglutarate As Co-Substrate (pdb code 4y5s). 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 with A-Ketoglutarate As Co-Substrate, PDB code: 4y5s:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of FTMOX1 with A-Ketoglutarate As Co-Substrate


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 with A-Ketoglutarate As Co-Substrate within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe402 b:26.5 occ:1.00 O2 A:AKG401 2.1 40.2 1.0 O5 A:AKG401 2.1 39.9 1.0 OD1 A:ASP135 2.1 32.5 1.0 NE2 A:HIS133 2.2 27.4 1.0 NE2 A:HIS209 2.2 32.5 1.0 O A:HOH507 2.5 24.2 1.0 OD2 A:ASP135 2.7 31.4 1.0 CG A:ASP135 2.7 30.5 1.0 C2 A:AKG401 2.8 41.6 1.0 C1 A:AKG401 2.8 41.3 1.0 CE1 A:HIS209 3.0 27.5 1.0 CE1 A:HIS133 3.1 29.7 1.0 CD2 A:HIS133 3.2 28.9 1.0 CD2 A:HIS209 3.2 26.8 1.0 O1 A:AKG401 4.0 38.4 1.0 ND1 A:HIS209 4.1 25.7 1.0 OH A:TYR228 4.2 37.4 1.0 CB A:ASP135 4.2 20.3 1.0 ND1 A:HIS133 4.2 32.0 1.0 CG A:HIS209 4.3 23.7 1.0 CG A:HIS133 4.3 26.4 1.0 C3 A:AKG401 4.3 38.4 1.0 CA A:ASP135 4.7 25.3 1.0 C4 A:AKG401 4.9 33.5 1.0 N A:ASP135 4.9 33.1 1.0

Iron binding site 2 out of 2 in the Structure of FTMOX1 with A-Ketoglutarate As Co-Substrate


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 with A-Ketoglutarate As Co-Substrate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe402 b:30.8 occ:1.00 OD1 B:ASP135 2.0 33.9 1.0 O1 B:AKG401 2.0 41.6 1.0 O5 B:AKG401 2.1 39.8 1.0 NE2 B:HIS209 2.2 33.1 1.0 NE2 B:HIS133 2.2 29.1 1.0 O B:HOH524 2.5 36.1 1.0 CG B:ASP135 2.7 42.2 1.0 C1 B:AKG401 2.7 43.9 1.0 C2 B:AKG401 2.7 43.2 1.0 OD2 B:ASP135 2.7 37.5 1.0 CE1 B:HIS209 2.9 36.1 1.0 CE1 B:HIS133 3.0 34.1 1.0 CD2 B:HIS209 3.2 31.4 1.0 CD2 B:HIS133 3.2 33.4 1.0 O2 B:AKG401 4.0 43.5 1.0 ND1 B:HIS209 4.1 33.4 1.0 OH B:TYR228 4.2 34.7 1.0 CB B:ASP135 4.2 32.1 1.0 ND1 B:HIS133 4.2 32.5 1.0 C3 B:AKG401 4.2 41.0 1.0 CG B:HIS209 4.2 32.4 1.0 CG B:HIS133 4.3 29.3 1.0 CA B:ASP135 4.8 33.1 1.0 C4 B:AKG401 4.9 39.5 1.0 N B:ASP135 4.9 31.3 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