Iron in PDB 1t93: Evidence For Multiple Substrate Recognition and Molecular Mechanism of C-C Reaction By Cytochrome P450 CYP158A2 From Streptomyces Coelicolor A3(2)

The structure of Evidence For Multiple Substrate Recognition and Molecular Mechanism of C-C Reaction By Cytochrome P450 CYP158A2 From Streptomyces Coelicolor A3(2), PDB code: 1t93 was solved by B.Zhao, M.Sundaramoorthy, M.R.Waterman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 1.62
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.800, 70.742, 102.576, 90.00, 90.00, 90.00
R / Rfree (%)	24.5 / 27.8

The binding sites of Iron atom in the Evidence For Multiple Substrate Recognition and Molecular Mechanism of C-C Reaction By Cytochrome P450 CYP158A2 From Streptomyces Coelicolor A3(2) (pdb code 1t93). 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 Evidence For Multiple Substrate Recognition and Molecular Mechanism of C-C Reaction By Cytochrome P450 CYP158A2 From Streptomyces Coelicolor A3(2), PDB code: 1t93:

Iron binding site 1 out of 1 in the Evidence For Multiple Substrate Recognition and Molecular Mechanism of C-C Reaction By Cytochrome P450 CYP158A2 From Streptomyces Coelicolor A3(2)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Evidence For Multiple Substrate Recognition and Molecular Mechanism of C-C Reaction By Cytochrome P450 CYP158A2 From Streptomyces Coelicolor A3(2) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe430 b:13.6 occ:1.00 FE A:HEM430 0.0 13.6 1.0 ND A:HEM430 2.0 11.7 1.0 NC A:HEM430 2.0 13.3 1.0 NB A:HEM430 2.0 14.8 1.0 NA A:HEM430 2.0 12.6 1.0 SG A:CYS353 2.4 13.3 1.0 C1C A:HEM430 3.0 14.7 1.0 C1D A:HEM430 3.0 12.4 1.0 C4C A:HEM430 3.0 12.0 1.0 C4D A:HEM430 3.1 10.6 1.0 C1B A:HEM430 3.1 13.8 1.0 C1A A:HEM430 3.1 11.0 1.0 C4A A:HEM430 3.1 13.6 1.0 C4B A:HEM430 3.1 15.5 1.0 CB A:CYS353 3.3 14.7 1.0 CHD A:HEM430 3.4 10.7 1.0 CHC A:HEM430 3.4 14.4 1.0 CHB A:HEM430 3.4 14.1 1.0 CHA A:HEM430 3.4 11.3 1.0 CA A:CYS353 4.2 14.0 1.0 O A:HOH505 4.2 17.6 1.0 C2C A:HEM430 4.3 12.8 1.0 C3C A:HEM430 4.3 13.0 1.0 C2D A:HEM430 4.3 12.2 1.0 C3D A:HEM430 4.3 12.4 1.0 C3A A:HEM430 4.3 13.0 1.0 C2A A:HEM430 4.3 13.6 1.0 C3B A:HEM430 4.3 14.5 1.0 C2B A:HEM430 4.3 15.6 1.0 CAF A:FLV431 4.6 13.9 1.0 O A:HOH600 5.0 25.2 1.0 C A:CYS353 5.0 13.1 1.0 OAC A:FLV431 5.0 15.5 1.0

B.Zhao, F.P.Guengerich, A.Bellamine, D.C.Lamb, M.Izumikawa, L.Lei, L.M.Podust, M.Sundaramoorthy, J.A.Kalaitzis, L.M.Reddy, S.L.Kelly, B.S.Moore, D.Stec, M.Voehler, J.R.Falck, T.Shimada, M.R.Waterman. Binding of Two Flaviolin Substrate Molecules, Oxidative Coupling, and Crystal Structure of Streptomyces Coelicolor A3(2) Cytochrome P450 158A2. J.Biol.Chem. V. 280 11599 2005.
ISSN: ISSN 0021-9258
PubMed: 15659395
DOI: 10.1074/JBC.M410933200