Iron in PDB 3el3: Distinct Monooxygenase and Farnesene Synthase Active Sites in Cytochrome P450 170A1

The structure of Distinct Monooxygenase and Farnesene Synthase Active Sites in Cytochrome P450 170A1, PDB code: 3el3 was solved by B.Zhao, M.R.Waterman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.48 / 3.30
Space group	P 63
Cell size a, b, c (Å), α, β, γ (°)	107.548, 107.548, 141.648, 90.00, 90.00, 120.00
R / Rfree (%)	22.8 / 26.5

The binding sites of Iron atom in the Distinct Monooxygenase and Farnesene Synthase Active Sites in Cytochrome P450 170A1 (pdb code 3el3). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Distinct Monooxygenase and Farnesene Synthase Active Sites in Cytochrome P450 170A1, PDB code: 3el3:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Distinct Monooxygenase and Farnesene Synthase Active Sites in Cytochrome P450 170A1


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Distinct Monooxygenase and Farnesene Synthase Active Sites in Cytochrome P450 170A1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:66.6 occ:1.00 FE A:HEM500 0.0 66.6 1.0 ND A:HEM500 2.0 68.5 1.0 NB A:HEM500 2.0 63.6 1.0 NC A:HEM500 2.0 65.9 1.0 NA A:HEM500 2.0 65.7 1.0 SG A:CYS410 2.4 70.8 1.0 C1B A:HEM500 3.0 62.7 1.0 C4D A:HEM500 3.0 70.2 1.0 C4A A:HEM500 3.0 65.3 1.0 C1D A:HEM500 3.0 69.0 1.0 C1A A:HEM500 3.1 66.8 1.0 C4B A:HEM500 3.1 63.2 1.0 C1C A:HEM500 3.1 66.0 1.0 C4C A:HEM500 3.1 66.7 1.0 CHB A:HEM500 3.4 63.7 1.0 CHA A:HEM500 3.4 68.0 1.0 CHD A:HEM500 3.4 66.2 1.0 CHC A:HEM500 3.4 63.7 1.0 CB A:CYS410 3.6 72.4 1.0 C2B A:HEM500 4.2 61.0 1.0 C3D A:HEM500 4.3 71.4 1.0 C3B A:HEM500 4.3 62.1 1.0 C2D A:HEM500 4.3 70.1 1.0 C3A A:HEM500 4.3 65.5 1.0 C2A A:HEM500 4.3 66.3 1.0 C2C A:HEM500 4.3 66.0 1.0 C3C A:HEM500 4.3 66.4 1.0 CA A:CYS410 4.4 73.3 1.0

Iron binding site 2 out of 2 in the Distinct Monooxygenase and Farnesene Synthase Active Sites in Cytochrome P450 170A1


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Distinct Monooxygenase and Farnesene Synthase Active Sites in Cytochrome P450 170A1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:58.3 occ:1.00 FE B:HEM500 0.0 58.3 1.0 ND B:HEM500 2.0 59.3 1.0 NC B:HEM500 2.0 58.6 1.0 NB B:HEM500 2.0 57.2 1.0 NA B:HEM500 2.0 59.1 1.0 SG B:CYS410 2.5 82.9 1.0 C1B B:HEM500 3.0 56.9 1.0 C4D B:HEM500 3.0 60.1 1.0 C1D B:HEM500 3.0 59.3 1.0 C1A B:HEM500 3.0 59.9 1.0 C4A B:HEM500 3.0 59.4 1.0 C1C B:HEM500 3.1 60.0 1.0 C4C B:HEM500 3.1 59.8 1.0 C4B B:HEM500 3.1 57.0 1.0 CHB B:HEM500 3.4 58.1 1.0 CHA B:HEM500 3.4 59.3 1.0 CHD B:HEM500 3.4 58.5 1.0 CHC B:HEM500 3.4 58.3 1.0 CB B:CYS410 3.8 82.0 1.0 C2B B:HEM500 4.3 55.3 1.0 C2D B:HEM500 4.3 59.6 1.0 C3A B:HEM500 4.3 60.0 1.0 C2A B:HEM500 4.3 60.9 1.0 C3D B:HEM500 4.3 60.0 1.0 C3B B:HEM500 4.3 56.1 1.0 CAE B:EL3501 4.3 0.3 1.0 C3C B:HEM500 4.3 60.0 1.0 C2C B:HEM500 4.3 60.0 1.0 CA B:CYS410 4.6 82.3 1.0

B.Zhao, L.Lei, D.G.Vassylyev, X.Lin, D.E.Cane, S.L.Kelly, H.Yuan, D.C.Lamb, M.R.Waterman. Crystal Structure of Albaflavenone Monooxygenase Containing A Moonlighting Terpene Synthase Active Site J.Biol.Chem. V. 284 36711 2009.
ISSN: ISSN 0021-9258
PubMed: 19858213
DOI: 10.1074/JBC.M109.064683