Iron in PDB 2ij3: Structure of the A264H Mutant of Cytochrome P450 BM3

All present enzymatic activity of Structure of the A264H Mutant of Cytochrome P450 BM3:
1.14.14.1;

The structure of Structure of the A264H Mutant of Cytochrome P450 BM3, PDB code: 2ij3 was solved by H.S.Toogood, D.Leys, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.98 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	58.703, 155.173, 62.198, 90.00, 94.19, 90.00
R / Rfree (%)	17.7 / 21.8

The binding sites of Iron atom in the Structure of the A264H Mutant of Cytochrome P450 BM3 (pdb code 2ij3). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of the A264H Mutant of Cytochrome P450 BM3, PDB code: 2ij3:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of the A264H Mutant of Cytochrome P450 BM3


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of the A264H Mutant of Cytochrome P450 BM3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe999 b:18.9 occ:1.00 FE A:HEM999 0.0 18.9 1.0 NC A:HEM999 2.1 18.5 1.0 NB A:HEM999 2.1 19.6 1.0 NA A:HEM999 2.1 18.5 1.0 ND A:HEM999 2.1 19.2 1.0 NE2 A:HIS264 2.2 21.4 1.0 SG A:CYS400 2.3 17.5 1.0 CD2 A:HIS264 3.0 21.3 1.0 C4B A:HEM999 3.1 19.6 1.0 C4C A:HEM999 3.1 18.0 1.0 C1C A:HEM999 3.1 17.9 1.0 C1A A:HEM999 3.1 19.1 1.0 C1B A:HEM999 3.1 19.0 1.0 C1D A:HEM999 3.1 18.0 1.0 C4D A:HEM999 3.1 19.2 1.0 C4A A:HEM999 3.1 18.6 1.0 CE1 A:HIS264 3.2 21.6 1.0 CB A:CYS400 3.3 16.5 1.0 CHC A:HEM999 3.4 18.0 1.0 CHD A:HEM999 3.4 18.1 1.0 CHA A:HEM999 3.4 17.1 1.0 CHB A:HEM999 3.5 18.2 1.0 CA A:CYS400 4.0 17.2 1.0 CG A:HIS264 4.2 20.1 1.0 ND1 A:HIS264 4.3 20.9 1.0 C3B A:HEM999 4.3 20.4 1.0 C3C A:HEM999 4.3 19.0 1.0 C2B A:HEM999 4.3 19.4 1.0 C2C A:HEM999 4.3 18.0 1.0 C2A A:HEM999 4.3 18.3 1.0 C3A A:HEM999 4.3 18.3 1.0 C3D A:HEM999 4.3 17.2 1.0 C2D A:HEM999 4.4 18.8 1.0 N A:GLY402 4.8 18.2 1.0 C A:CYS400 4.8 17.8 1.0

Iron binding site 2 out of 2 in the Structure of the A264H Mutant of Cytochrome P450 BM3


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of the A264H Mutant of Cytochrome P450 BM3 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe999 b:20.1 occ:1.00 FE B:HEM999 0.0 20.1 1.0 NB B:HEM999 2.0 19.3 1.0 NA B:HEM999 2.1 18.7 1.0 NC B:HEM999 2.1 18.1 1.0 ND B:HEM999 2.1 20.5 1.0 NE2 B:HIS264 2.1 21.1 1.0 SG B:CYS400 2.2 19.1 1.0 C4A B:HEM999 3.1 19.4 1.0 C1B B:HEM999 3.1 19.2 1.0 CD2 B:HIS264 3.1 23.1 1.0 C4C B:HEM999 3.1 19.7 1.0 C4B B:HEM999 3.1 20.0 1.0 C1D B:HEM999 3.1 19.9 1.0 C1A B:HEM999 3.1 19.6 1.0 C1C B:HEM999 3.1 19.2 1.0 C4D B:HEM999 3.1 20.2 1.0 CE1 B:HIS264 3.2 22.5 1.0 CB B:CYS400 3.4 20.2 1.0 CHB B:HEM999 3.4 17.6 1.0 CHD B:HEM999 3.4 19.4 1.0 CHC B:HEM999 3.5 18.6 1.0 CHA B:HEM999 3.5 18.7 1.0 CA B:CYS400 4.0 20.4 1.0 CG B:HIS264 4.2 22.9 1.0 ND1 B:HIS264 4.2 21.3 1.0 C2B B:HEM999 4.3 19.3 1.0 C3A B:HEM999 4.3 18.1 1.0 C3B B:HEM999 4.3 19.4 1.0 C3C B:HEM999 4.3 20.0 1.0 C2A B:HEM999 4.3 19.6 1.0 C2C B:HEM999 4.3 17.9 1.0 C2D B:HEM999 4.3 19.5 1.0 C3D B:HEM999 4.3 19.0 1.0 N B:GLY402 4.8 20.6 1.0 C B:CYS400 4.8 20.9 1.0

H.M.Girvan, H.E.Seward, H.S.Toogood, M.R.Cheesman, D.Leys, A.W.Munro. Structural and Spectroscopic Characterization of P450 BM3 Mutants with Unprecedented P450 Heme Iron Ligand Sets. New Heme Ligation States Influence Conformational Equilibria in P450 BM3. J.Biol.Chem. V. 282 564 2007.
ISSN: ISSN 0021-9258
PubMed: 17077084
DOI: 10.1074/JBC.M607949200