Iron in PDB 1smi: A Single Mutation of P450 BM3 Induces the Conformational Rearrangement Seen Upon Substrate-Binding in Wild-Type Enzyme

All present enzymatic activity of A Single Mutation of P450 BM3 Induces the Conformational Rearrangement Seen Upon Substrate-Binding in Wild-Type Enzyme:
1.14.14.1;

The structure of A Single Mutation of P450 BM3 Induces the Conformational Rearrangement Seen Upon Substrate-Binding in Wild-Type Enzyme, PDB code: 1smi was solved by M.G.Joyce, H.M.Girvan, A.W.Munro, D.Leys, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	14.92 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	61.206, 118.929, 146.338, 90.00, 90.00, 90.00
R / Rfree (%)	22.4 / 28.8

The binding sites of Iron atom in the A Single Mutation of P450 BM3 Induces the Conformational Rearrangement Seen Upon Substrate-Binding in Wild-Type Enzyme (pdb code 1smi). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the A Single Mutation of P450 BM3 Induces the Conformational Rearrangement Seen Upon Substrate-Binding in Wild-Type Enzyme, PDB code: 1smi:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the A Single Mutation of P450 BM3 Induces the Conformational Rearrangement Seen Upon Substrate-Binding in Wild-Type Enzyme


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of A Single Mutation of P450 BM3 Induces the Conformational Rearrangement Seen Upon Substrate-Binding in Wild-Type Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe472 b:28.3 occ:1.00 FE A:HEM472 0.0 28.3 1.0 OE1 A:GLU264 1.9 40.9 1.0 NC A:HEM472 2.0 26.2 1.0 NA A:HEM472 2.0 27.4 1.0 ND A:HEM472 2.1 26.2 1.0 NB A:HEM472 2.1 26.2 1.0 SG A:CYS400 2.3 28.4 1.0 C4C A:HEM472 3.0 27.9 1.0 C4A A:HEM472 3.0 28.6 1.0 C1D A:HEM472 3.0 28.1 1.0 C1B A:HEM472 3.1 27.5 1.0 C1C A:HEM472 3.1 25.6 1.0 C1A A:HEM472 3.1 27.6 1.0 C4B A:HEM472 3.1 22.8 1.0 CD A:GLU264 3.1 46.5 1.0 C4D A:HEM472 3.2 27.5 1.0 CB A:CYS400 3.3 27.2 1.0 CHD A:HEM472 3.3 27.6 1.0 CHB A:HEM472 3.4 26.6 1.0 CHC A:HEM472 3.5 25.8 1.0 CHA A:HEM472 3.5 27.8 1.0 CA A:CYS400 4.0 28.3 1.0 OE2 A:GLU264 4.0 51.9 1.0 CG A:GLU264 4.0 44.7 1.0 C3C A:HEM472 4.2 27.9 1.0 C3A A:HEM472 4.2 28.5 1.0 C2A A:HEM472 4.3 26.9 1.0 C2C A:HEM472 4.3 27.1 1.0 C3B A:HEM472 4.3 21.1 1.0 C2D A:HEM472 4.3 26.1 1.0 C2B A:HEM472 4.3 25.9 1.0 C3D A:HEM472 4.4 24.0 1.0 N A:GLY402 4.8 29.4 1.0 C A:CYS400 4.8 29.2 1.0 CE2 A:PHE87 4.9 43.2 1.0 CB A:GLU264 4.9 42.5 1.0 O A:GLU264 4.9 41.1 1.0 N A:ILE401 4.9 28.7 1.0

Iron binding site 2 out of 2 in the A Single Mutation of P450 BM3 Induces the Conformational Rearrangement Seen Upon Substrate-Binding in Wild-Type Enzyme


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of A Single Mutation of P450 BM3 Induces the Conformational Rearrangement Seen Upon Substrate-Binding in Wild-Type Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe472 b:35.2 occ:1.00 FE B:HEM472 0.0 35.2 1.0 NB B:HEM472 1.9 34.2 1.0 ND B:HEM472 2.0 34.4 1.0 NA B:HEM472 2.1 31.7 1.0 NC B:HEM472 2.1 34.5 1.0 SG B:CYS400 2.5 34.6 1.0 O B:HOH496 2.6 46.7 1.0 C4B B:HEM472 3.0 36.9 1.0 C1D B:HEM472 3.0 36.7 1.0 C1B B:HEM472 3.0 35.5 1.0 C4A B:HEM472 3.0 29.3 1.0 C4D B:HEM472 3.1 34.0 1.0 C4C B:HEM472 3.1 31.9 1.0 C1A B:HEM472 3.1 31.6 1.0 C1C B:HEM472 3.1 33.1 1.0 CB B:CYS400 3.3 33.2 1.0 CHD B:HEM472 3.4 34.8 1.0 CHB B:HEM472 3.4 33.0 1.0 CHC B:HEM472 3.4 34.2 1.0 CHA B:HEM472 3.4 33.8 1.0 CA B:CYS400 4.0 35.1 1.0 C3B B:HEM472 4.2 35.2 1.0 C2B B:HEM472 4.2 34.9 1.0 C2D B:HEM472 4.2 34.6 1.0 C3D B:HEM472 4.3 35.0 1.0 C3A B:HEM472 4.3 32.8 1.0 C2A B:HEM472 4.3 31.4 1.0 C3C B:HEM472 4.3 33.6 1.0 C2C B:HEM472 4.3 35.4 1.0 C B:CYS400 4.8 36.0 1.0 N B:GLY402 4.9 36.4 1.0 CB B:GLU264 4.9 50.0 1.0 CE1 B:PHE87 4.9 43.1 1.0 O B:GLU264 4.9 50.0 1.0

M.G.Joyce, H.M.Girvan, A.W.Munro, D.Leys. A Single Mutation in Cytochrome P450 BM3 Induces the Conformational Rearrangement Seen Upon Substrate Binding in the Wild-Type Enzyme J.Biol.Chem. V. 279 23287 2004.
ISSN: ISSN 0021-9258
PubMed: 15020590
DOI: 10.1074/JBC.M401717200