Iron in PDB 1smj: Structure of the A264E Mutant of Cytochrome P450 BM3 Complexed with Palmitoleate

All present enzymatic activity of Structure of the A264E Mutant of Cytochrome P450 BM3 Complexed with Palmitoleate:
1.14.14.1;

The structure of Structure of the A264E Mutant of Cytochrome P450 BM3 Complexed with Palmitoleate, PDB code: 1smj 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)	15.00 / 2.75
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	107.312, 166.886, 224.937, 90.00, 90.00, 90.00
R / Rfree (%)	25.3 / 33.8

The binding sites of Iron atom in the Structure of the A264E Mutant of Cytochrome P450 BM3 Complexed with Palmitoleate (pdb code 1smj). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Structure of the A264E Mutant of Cytochrome P450 BM3 Complexed with Palmitoleate, PDB code: 1smj:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Structure of the A264E Mutant of Cytochrome P450 BM3 Complexed with Palmitoleate


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 A264E Mutant of Cytochrome P450 BM3 Complexed with Palmitoleate within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe472 b:36.2 occ:1.00 FE A:HEM472 0.0 36.2 1.0 OE2 A:GLU264 1.8 46.6 1.0 NA A:HEM472 1.8 21.9 1.0 NC A:HEM472 1.9 24.3 1.0 NB A:HEM472 2.0 31.7 1.0 ND A:HEM472 2.1 28.2 1.0 SG A:CYS400 2.3 35.8 1.0 CD A:GLU264 2.9 51.3 1.0 C4A A:HEM472 2.9 27.9 1.0 C1A A:HEM472 2.9 26.6 1.0 C4C A:HEM472 2.9 26.0 1.0 C1C A:HEM472 3.0 28.3 1.0 C1B A:HEM472 3.0 32.2 1.0 C4B A:HEM472 3.1 31.8 1.0 CB A:CYS400 3.1 35.2 1.0 C1D A:HEM472 3.1 26.3 1.0 C4D A:HEM472 3.1 30.6 1.0 CHD A:HEM472 3.3 27.3 1.0 CHB A:HEM472 3.4 28.6 1.0 CHA A:HEM472 3.4 26.5 1.0 CHC A:HEM472 3.4 30.3 1.0 OE1 A:GLU264 3.7 46.2 1.0 CG A:GLU264 3.9 44.5 1.0 CA A:CYS400 3.9 37.4 1.0 C2A A:HEM472 4.1 26.3 1.0 C3A A:HEM472 4.1 26.3 1.0 C3C A:HEM472 4.1 26.8 1.0 C2C A:HEM472 4.2 27.6 1.0 C2B A:HEM472 4.2 28.6 1.0 C3B A:HEM472 4.2 32.0 1.0 C3D A:HEM472 4.4 31.2 1.0 C2D A:HEM472 4.4 26.8 1.0 CE2 A:PHE87 4.4 38.4 1.0 O A:GLU264 4.5 40.7 1.0 C A:CYS400 4.8 37.8 1.0 N A:GLY402 4.8 38.7 1.0

Iron binding site 2 out of 4 in the Structure of the A264E Mutant of Cytochrome P450 BM3 Complexed with Palmitoleate


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 A264E Mutant of Cytochrome P450 BM3 Complexed with Palmitoleate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe472 b:50.9 occ:1.00 FE B:HEM472 0.0 50.9 1.0 NC B:HEM472 1.8 27.3 1.0 NB B:HEM472 1.9 37.9 1.0 NA B:HEM472 1.9 34.6 1.0 ND B:HEM472 2.0 33.5 1.0 OE2 B:GLU264 2.3 68.8 1.0 SG B:CYS400 2.4 64.5 1.0 C1C B:HEM472 2.7 33.8 1.0 C4B B:HEM472 2.8 40.9 1.0 C4C B:HEM472 2.9 32.7 1.0 C1A B:HEM472 2.9 32.8 1.0 C4A B:HEM472 3.0 37.5 1.0 C4D B:HEM472 3.0 35.5 1.0 C1B B:HEM472 3.0 37.2 1.0 CHC B:HEM472 3.1 37.0 1.0 C1D B:HEM472 3.1 36.1 1.0 CHA B:HEM472 3.3 34.0 1.0 CB B:CYS400 3.3 59.3 1.0 CD B:GLU264 3.4 64.9 1.0 CHB B:HEM472 3.4 32.5 1.0 CHD B:HEM472 3.5 33.7 1.0 CG B:GLU264 3.8 51.5 1.0 C2C B:HEM472 4.0 31.0 1.0 CA B:CYS400 4.1 59.6 1.0 C3C B:HEM472 4.1 29.4 1.0 C3B B:HEM472 4.1 35.3 1.0 CE2 B:PHE87 4.2 37.5 1.0 C2A B:HEM472 4.2 34.0 1.0 C3A B:HEM472 4.2 39.7 1.0 C2B B:HEM472 4.2 32.5 1.0 C3D B:HEM472 4.3 38.7 1.0 C2D B:HEM472 4.3 33.2 1.0 O B:GLU264 4.4 37.8 1.0 OE1 B:GLU264 4.5 71.4 1.0 C B:CYS400 4.7 60.3 1.0 CD2 B:PHE87 4.9 40.9 1.0 OG1 B:THR268 4.9 57.8 1.0 N B:GLY402 4.9 54.8 1.0 N B:ILE401 4.9 61.0 1.0 CD1 B:PHE393 5.0 47.0 1.0

Iron binding site 3 out of 4 in the Structure of the A264E Mutant of Cytochrome P450 BM3 Complexed with Palmitoleate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structure of the A264E Mutant of Cytochrome P450 BM3 Complexed with Palmitoleate within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe472 b:41.1 occ:1.00 FE C:HEM472 0.0 41.1 1.0 NA C:HEM472 1.8 23.7 1.0 NC C:HEM472 1.9 24.2 1.0 ND C:HEM472 1.9 30.6 1.0 OE2 C:GLU264 2.0 65.7 1.0 NB C:HEM472 2.1 29.4 1.0 SG C:CYS400 2.8 50.3 1.0 C4C C:HEM472 2.8 27.0 1.0 C4D C:HEM472 2.8 37.1 1.0 C4A C:HEM472 2.9 28.0 1.0 C1A C:HEM472 2.9 30.5 1.0 C1D C:HEM472 2.9 35.2 1.0 C1C C:HEM472 3.0 27.4 1.0 C1B C:HEM472 3.1 28.1 1.0 CD C:GLU264 3.2 63.5 1.0 C4B C:HEM472 3.2 32.7 1.0 CHA C:HEM472 3.3 31.6 1.0 CB C:CYS400 3.3 50.9 1.0 CHD C:HEM472 3.3 31.5 1.0 CHB C:HEM472 3.4 25.3 1.0 CHC C:HEM472 3.6 29.1 1.0 CG C:GLU264 3.7 50.4 1.0 CA C:CYS400 4.0 52.1 1.0 C3C C:HEM472 4.1 27.3 1.0 C3D C:HEM472 4.1 41.1 1.0 C2D C:HEM472 4.1 37.2 1.0 C3A C:HEM472 4.1 30.5 1.0 C2C C:HEM472 4.1 26.4 1.0 C2A C:HEM472 4.2 27.1 1.0 OE1 C:GLU264 4.3 65.2 1.0 C2B C:HEM472 4.3 29.2 1.0 C3B C:HEM472 4.4 30.4 1.0 CE2 C:PHE87 4.6 43.3 1.0 O C:GLU264 4.6 37.5 1.0 N C:GLY402 4.7 52.8 1.0 C C:CYS400 4.8 50.9 1.0 CA C:GLY402 5.0 54.4 1.0

Iron binding site 4 out of 4 in the Structure of the A264E Mutant of Cytochrome P450 BM3 Complexed with Palmitoleate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structure of the A264E Mutant of Cytochrome P450 BM3 Complexed with Palmitoleate within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe472 b:48.6 occ:1.00 FE D:HEM472 0.0 48.6 1.0 NB D:HEM472 1.8 38.0 1.0 OE2 D:GLU264 2.0 56.1 1.0 NC D:HEM472 2.1 34.2 1.0 NA D:HEM472 2.1 42.3 1.0 ND D:HEM472 2.1 41.8 1.0 SG D:CYS400 2.2 60.3 1.0 C4B D:HEM472 2.9 38.8 1.0 C1B D:HEM472 2.9 40.5 1.0 CB D:CYS400 3.0 56.6 1.0 C4A D:HEM472 3.1 44.2 1.0 C4C D:HEM472 3.1 31.3 1.0 C1C D:HEM472 3.1 34.2 1.0 C1D D:HEM472 3.1 40.0 1.0 C4D D:HEM472 3.1 45.6 1.0 C1A D:HEM472 3.2 44.8 1.0 CD D:GLU264 3.2 58.7 1.0 CHB D:HEM472 3.3 42.4 1.0 CHC D:HEM472 3.3 37.4 1.0 CHD D:HEM472 3.5 36.4 1.0 CHA D:HEM472 3.5 44.4 1.0 CA D:CYS400 3.9 56.5 1.0 CG D:GLU264 3.9 52.4 1.0 C3B D:HEM472 4.1 38.6 1.0 C2B D:HEM472 4.1 36.4 1.0 C3C D:HEM472 4.3 32.6 1.0 C2C D:HEM472 4.3 29.4 1.0 OE1 D:GLU264 4.3 65.8 1.0 C3A D:HEM472 4.3 39.6 1.0 C2D D:HEM472 4.4 37.4 1.0 C3D D:HEM472 4.4 46.3 1.0 C2A D:HEM472 4.4 42.5 1.0 N D:GLY402 4.5 54.1 1.0 CA D:GLY402 4.6 54.5 1.0 C D:CYS400 4.6 55.2 1.0 O D:GLU264 4.6 50.2 1.0 N D:GLN403 4.8 55.6 1.0 N D:ILE401 5.0 54.3 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