Iron in PDB 4hgi: Crystal Structure of P450 BM3 5F5 Heme Domain Variant Complexed with Styrene (Dataset II)

All present enzymatic activity of Crystal Structure of P450 BM3 5F5 Heme Domain Variant Complexed with Styrene (Dataset II):
1.14.14.1; 1.6.2.4;

The structure of Crystal Structure of P450 BM3 5F5 Heme Domain Variant Complexed with Styrene (Dataset II), PDB code: 4hgi 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)	19.99 / 1.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	58.990, 148.890, 64.820, 90.00, 98.37, 90.00
R / Rfree (%)	17.8 / 19.9

The binding sites of Iron atom in the Crystal Structure of P450 BM3 5F5 Heme Domain Variant Complexed with Styrene (Dataset II) (pdb code 4hgi). 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 5F5 Heme Domain Variant Complexed with Styrene (Dataset II), PDB code: 4hgi:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of P450 BM3 5F5 Heme Domain Variant Complexed with Styrene (Dataset II)


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 5F5 Heme Domain Variant Complexed with Styrene (Dataset II) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:8.6 occ:1.00 FE A:HEM501 0.0 8.6 1.0 NB A:HEM501 2.1 7.5 1.0 NC A:HEM501 2.1 10.0 1.0 NA A:HEM501 2.1 8.3 1.0 ND A:HEM501 2.1 7.5 1.0 O A:HOH1056 2.2 21.2 0.5 SG A:CYS400 2.3 9.8 1.0 CAA A:SYN502 2.6 20.4 0.5 C4B A:HEM501 3.0 9.1 1.0 C1B A:HEM501 3.0 9.1 1.0 C1C A:HEM501 3.0 8.0 1.0 C4A A:HEM501 3.1 8.1 1.0 C4C A:HEM501 3.1 8.4 1.0 C4D A:HEM501 3.1 8.0 1.0 C1D A:HEM501 3.1 8.4 1.0 C1A A:HEM501 3.1 5.4 1.0 CB A:CYS400 3.3 8.4 1.0 CHC A:HEM501 3.4 10.4 1.0 CHB A:HEM501 3.4 9.1 1.0 CHD A:HEM501 3.5 11.7 1.0 CHA A:HEM501 3.5 6.9 1.0 CAB A:SYN502 3.9 20.6 0.5 CA A:CYS400 3.9 6.9 1.0 C3B A:HEM501 4.2 8.2 1.0 C2B A:HEM501 4.2 8.7 1.0 C2C A:HEM501 4.3 8.7 1.0 C3A A:HEM501 4.3 7.4 1.0 C3C A:HEM501 4.3 10.5 1.0 O A:ALA264 4.3 17.0 1.0 C2A A:HEM501 4.3 6.2 1.0 C2D A:HEM501 4.3 8.1 1.0 C3D A:HEM501 4.3 7.4 1.0 CAG A:SYN502 4.6 22.0 0.5 CB A:ALA264 4.7 17.4 1.0 CAH A:SYN502 4.8 18.0 0.5 C A:CYS400 4.8 6.6 1.0 N A:GLY402 4.8 8.3 1.0 CAE A:SYN502 4.9 24.5 0.5 CAC A:SYN502 4.9 24.3 0.5 N A:ILE401 5.0 7.8 1.0 C A:ALA264 5.0 16.2 1.0

Iron binding site 2 out of 2 in the Crystal Structure of P450 BM3 5F5 Heme Domain Variant Complexed with Styrene (Dataset II)


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 5F5 Heme Domain Variant Complexed with Styrene (Dataset II) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe502 b:9.3 occ:1.00 FE B:HEM502 0.0 9.3 1.0 ND B:HEM502 2.1 8.9 1.0 NA B:HEM502 2.1 7.8 1.0 NC B:HEM502 2.1 7.9 1.0 NB B:HEM502 2.2 7.3 1.0 SG B:CYS400 2.3 10.4 1.0 O B:HOH1005 2.4 13.9 0.5 CAA B:SYN503 2.9 21.5 0.5 C4D B:HEM502 3.0 8.1 1.0 C1D B:HEM502 3.0 8.1 1.0 C1A B:HEM502 3.1 7.3 1.0 C4A B:HEM502 3.1 7.5 1.0 C4C B:HEM502 3.1 8.8 1.0 C1B B:HEM502 3.1 7.5 1.0 C1C B:HEM502 3.1 9.9 1.0 C4B B:HEM502 3.1 8.9 1.0 CAB B:SYN503 3.2 22.3 0.5 CB B:CYS400 3.2 9.2 1.0 CHA B:HEM502 3.4 11.9 1.0 CHB B:HEM502 3.4 8.3 1.0 CHD B:HEM502 3.5 9.3 1.0 CHC B:HEM502 3.5 9.5 1.0 CA B:CYS400 3.9 9.0 1.0 CAH B:SYN503 4.1 25.5 0.5 CAG B:SYN503 4.2 24.7 0.5 C3D B:HEM502 4.3 9.4 1.0 C2D B:HEM502 4.3 8.3 1.0 C2A B:HEM502 4.3 9.0 1.0 C3A B:HEM502 4.3 8.2 1.0 C3C B:HEM502 4.3 10.5 1.0 C2C B:HEM502 4.3 11.5 1.0 C2B B:HEM502 4.3 8.0 1.0 C3B B:HEM502 4.3 9.4 1.0 O B:ALA264 4.3 18.1 1.0 C B:CYS400 4.7 8.9 1.0 N B:GLY402 4.8 8.5 1.0 CAD B:SYN503 4.8 24.6 0.5 N B:ILE401 4.9 8.8 1.0 CB B:ALA264 4.9 23.1 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