Iron in PDB 4fxb: Crystal Structure of CYP105N1 From Streptomyces Coelicolor: A Cytochrome P450 Oxidase in the Coelibactin Siderophore Biosynthetic Pathway

The structure of Crystal Structure of CYP105N1 From Streptomyces Coelicolor: A Cytochrome P450 Oxidase in the Coelibactin Siderophore Biosynthetic Pathway, PDB code: 4fxb was solved by M.K.Hong, Y.R.Lim, J.K.Kim, D.H.Kim, L.W.Kang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.93 / 2.90
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	133.086, 133.086, 227.111, 90.00, 90.00, 120.00
R / Rfree (%)	28.1 / 30.2

The binding sites of Iron atom in the Crystal Structure of CYP105N1 From Streptomyces Coelicolor: A Cytochrome P450 Oxidase in the Coelibactin Siderophore Biosynthetic Pathway (pdb code 4fxb). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of CYP105N1 From Streptomyces Coelicolor: A Cytochrome P450 Oxidase in the Coelibactin Siderophore Biosynthetic Pathway, PDB code: 4fxb:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of CYP105N1 From Streptomyces Coelicolor: A Cytochrome P450 Oxidase in the Coelibactin Siderophore Biosynthetic Pathway


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of CYP105N1 From Streptomyces Coelicolor: A Cytochrome P450 Oxidase in the Coelibactin Siderophore Biosynthetic Pathway within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:34.1 occ:1.00 FE A:HEM501 0.0 34.1 1.0 NA A:HEM501 2.1 30.0 1.0 NC A:HEM501 2.1 29.6 1.0 NB A:HEM501 2.1 31.6 1.0 ND A:HEM501 2.1 27.0 1.0 SG A:CYS360 2.1 21.3 1.0 C1A A:HEM501 3.1 29.4 1.0 C4C A:HEM501 3.1 28.1 1.0 C4A A:HEM501 3.1 32.4 1.0 C1C A:HEM501 3.1 32.3 1.0 C1D A:HEM501 3.1 28.7 1.0 C4D A:HEM501 3.1 28.1 1.0 C1B A:HEM501 3.1 34.4 1.0 C4B A:HEM501 3.1 35.5 1.0 CB A:CYS360 3.1 19.8 1.0 CHD A:HEM501 3.4 26.7 1.0 CHA A:HEM501 3.4 27.2 1.0 CHB A:HEM501 3.5 34.9 1.0 CHC A:HEM501 3.5 35.8 1.0 CA A:CYS360 3.8 19.9 1.0 C2A A:HEM501 4.3 29.9 1.0 C3A A:HEM501 4.3 29.4 1.0 C3C A:HEM501 4.3 28.9 1.0 C2C A:HEM501 4.3 29.0 1.0 C2B A:HEM501 4.3 34.3 1.0 C3B A:HEM501 4.3 36.1 1.0 C2D A:HEM501 4.3 32.5 1.0 C3D A:HEM501 4.3 31.3 1.0 C A:CYS360 4.5 17.4 1.0 N A:GLY362 4.8 16.7 1.0 CA A:GLY362 4.8 15.7 1.0 CB A:ALA249 4.9 24.8 1.0 O A:ALA249 5.0 23.5 1.0

Iron binding site 2 out of 2 in the Crystal Structure of CYP105N1 From Streptomyces Coelicolor: A Cytochrome P450 Oxidase in the Coelibactin Siderophore Biosynthetic Pathway


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of CYP105N1 From Streptomyces Coelicolor: A Cytochrome P450 Oxidase in the Coelibactin Siderophore Biosynthetic Pathway within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:29.9 occ:1.00 FE B:HEM501 0.0 29.9 1.0 NC B:HEM501 2.1 29.0 1.0 NA B:HEM501 2.1 25.4 1.0 NB B:HEM501 2.1 26.8 1.0 ND B:HEM501 2.1 31.7 1.0 SG B:CYS360 2.2 15.8 1.0 CB B:CYS360 3.0 18.5 1.0 C1A B:HEM501 3.1 28.5 1.0 C4C B:HEM501 3.1 32.7 1.0 C1C B:HEM501 3.1 29.4 1.0 C4A B:HEM501 3.1 25.8 1.0 C4D B:HEM501 3.1 33.7 1.0 C1D B:HEM501 3.1 33.0 1.0 C4B B:HEM501 3.1 28.4 1.0 C1B B:HEM501 3.1 26.4 1.0 CHA B:HEM501 3.4 35.1 1.0 CHD B:HEM501 3.4 33.3 1.0 CHC B:HEM501 3.5 26.4 1.0 CHB B:HEM501 3.5 26.4 1.0 CA B:CYS360 3.8 23.5 1.0 C3C B:HEM501 4.3 33.3 1.0 C2A B:HEM501 4.3 27.7 1.0 C2C B:HEM501 4.3 31.2 1.0 C3A B:HEM501 4.3 25.6 1.0 C3B B:HEM501 4.3 28.2 1.0 C2B B:HEM501 4.3 28.6 1.0 C3D B:HEM501 4.3 33.6 1.0 C2D B:HEM501 4.3 33.1 1.0 N B:CYS360 4.8 28.3 1.0 C B:CYS360 4.8 23.1 1.0 N B:GLY362 5.0 23.8 1.0 N B:VAL361 5.0 21.2 1.0

Y.R.Lim, M.K.Hong, J.K.Kim, T.T.Doan, D.H.Kim, C.H.Yun, Y.J.Chun, L.W.Kang, D.Kim. Crystal Structure of Cytochrome P450 CYP105N1 From Streptomyces Coelicolor, An Oxidase in the Coelibactin Siderophore Biosynthetic Pathway Arch.Biochem.Biophys. V. 528 111 2012.
ISSN: ISSN 0003-9861
PubMed: 23000034
DOI: 10.1016/J.ABB.2012.09.001