Iron in PDB 4hgf: Crystal Structure of P450 BM3 5F5K Heme Domain Variant Complexed with Styrene

All present enzymatic activity of Crystal Structure of P450 BM3 5F5K Heme Domain Variant Complexed with Styrene:
1.14.14.1; 1.6.2.4;

The structure of Crystal Structure of P450 BM3 5F5K Heme Domain Variant Complexed with Styrene, PDB code: 4hgf was solved by A.Shehzad, S.Panneerselvam, M.Bocola, J.Mueller-Dieckmann, M.Wilmanns, U.Schwaneberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.51 / 1.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	59.138, 148.125, 64.066, 90.00, 98.16, 90.00
R / Rfree (%)	18.9 / 22.8

The structure of Crystal Structure of P450 BM3 5F5K Heme Domain Variant Complexed with Styrene also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Iron atom in the Crystal Structure of P450 BM3 5F5K Heme Domain Variant Complexed with Styrene (pdb code 4hgf). 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 P450 BM3 5F5K Heme Domain Variant Complexed with Styrene, PDB code: 4hgf:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of P450 BM3 5F5K Heme Domain Variant Complexed with Styrene


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 P450 BM3 5F5K Heme Domain Variant Complexed with Styrene within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:10.9 occ:1.00 FE A:HEM501 0.0 10.9 1.0 NC A:HEM501 2.0 9.6 1.0 NB A:HEM501 2.1 10.1 1.0 ND A:HEM501 2.1 9.9 1.0 NA A:HEM501 2.2 10.0 1.0 SG A:CYS400 2.3 12.1 1.0 CAB A:SYN502 2.6 23.4 1.0 C4C A:HEM501 2.9 8.7 1.0 C1C A:HEM501 3.0 9.3 1.0 C1D A:HEM501 3.1 11.1 1.0 C4D A:HEM501 3.1 12.0 1.0 C1B A:HEM501 3.1 10.8 1.0 C4B A:HEM501 3.1 10.9 1.0 C1A A:HEM501 3.1 9.7 1.0 C4A A:HEM501 3.2 9.7 1.0 CHD A:HEM501 3.4 9.8 1.0 CHC A:HEM501 3.4 9.9 1.0 CB A:CYS400 3.4 10.5 1.0 CHA A:HEM501 3.4 10.9 1.0 CHB A:HEM501 3.5 9.8 1.0 CAA A:SYN502 3.6 19.7 1.0 CAH A:SYN502 3.6 29.7 1.0 CA A:CYS400 4.0 10.5 1.0 C3C A:HEM501 4.1 9.9 1.0 C2C A:HEM501 4.2 9.0 1.0 CAG A:SYN502 4.2 30.4 1.0 C2B A:HEM501 4.3 9.5 1.0 C3D A:HEM501 4.3 10.4 1.0 C2D A:HEM501 4.3 10.6 1.0 C3B A:HEM501 4.3 9.8 1.0 C2A A:HEM501 4.4 10.6 1.0 C3A A:HEM501 4.4 10.1 1.0 CAF A:SYN502 4.5 34.3 1.0 C A:CYS400 4.7 11.6 1.0 O A:ALA264 4.9 15.2 1.0 N A:GLY402 4.9 11.5 1.0 N A:ILE401 4.9 12.6 1.0

Iron binding site 2 out of 2 in the Crystal Structure of P450 BM3 5F5K Heme Domain Variant Complexed with Styrene


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 P450 BM3 5F5K Heme Domain Variant Complexed with Styrene within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:11.1 occ:1.00 FE B:HEM501 0.0 11.1 1.0 ND B:HEM501 2.1 10.0 1.0 NC B:HEM501 2.1 9.6 1.0 NB B:HEM501 2.1 9.5 1.0 NA B:HEM501 2.2 9.3 1.0 SG B:CYS400 2.3 11.0 1.0 CAB B:SYN502 2.4 25.0 1.0 C4C B:HEM501 3.0 9.7 1.0 C1C B:HEM501 3.0 9.3 1.0 C1D B:HEM501 3.0 10.7 1.0 C1B B:HEM501 3.0 9.4 1.0 C4D B:HEM501 3.1 9.5 1.0 C4B B:HEM501 3.1 9.4 1.0 C4A B:HEM501 3.1 8.7 1.0 C1A B:HEM501 3.1 8.7 1.0 CAH B:SYN502 3.3 32.8 1.0 CB B:CYS400 3.3 10.6 1.0 CHB B:HEM501 3.4 8.4 1.0 CHC B:HEM501 3.4 8.8 1.0 CHD B:HEM501 3.4 10.6 1.0 CHA B:HEM501 3.4 9.7 1.0 CAA B:SYN502 3.6 21.9 1.0 CAG B:SYN502 3.9 33.5 1.0 CA B:CYS400 4.0 11.3 1.0 CAF B:SYN502 4.2 29.7 1.0 C2B B:HEM501 4.3 9.0 1.0 C3C B:HEM501 4.3 10.9 1.0 C2C B:HEM501 4.3 11.1 1.0 C3B B:HEM501 4.3 9.8 1.0 C2D B:HEM501 4.3 10.1 1.0 C3A B:HEM501 4.3 8.7 1.0 C3D B:HEM501 4.3 10.2 1.0 C2A B:HEM501 4.3 9.2 1.0 C B:CYS400 4.8 12.4 1.0 N B:GLY402 4.9 11.8 1.0

A.Shehzad, S.Panneerselvam, M.Linow, M.Bocola, D.Roccatano, J.Mueller-Dieckmann, M.Wilmanns, U.Schwaneberg. P450 BM3 Crystal Structures Reveal the Role of the Charged Surface Residue Lys/ARG184 in Inversion of Enantioselective Styrene Epoxidation. Chem.Commun.(Camb.) V. 49 4694 2013.
ISSN: ISSN 1359-7345
PubMed: 23589805
DOI: 10.1039/C3CC39076D