Iron in PDB 5dyz: Crystal Structure of ASP251GLY/GLN307HIS Mutant of Cytochrome P450 BM3 in Complex with N-Palmitoylglycine

All present enzymatic activity of Crystal Structure of ASP251GLY/GLN307HIS Mutant of Cytochrome P450 BM3 in Complex with N-Palmitoylglycine:
1.14.14.1; 1.6.2.4;

The structure of Crystal Structure of ASP251GLY/GLN307HIS Mutant of Cytochrome P450 BM3 in Complex with N-Palmitoylglycine, PDB code: 5dyz was solved by G.Di Nardo, V.Dell'angelo, G.Gilardi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.54 / 1.97
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	61.213, 115.708, 143.278, 90.00, 90.00, 90.00
R / Rfree (%)	17.9 / 21.9

The binding sites of Iron atom in the Crystal Structure of ASP251GLY/GLN307HIS Mutant of Cytochrome P450 BM3 in Complex with N-Palmitoylglycine (pdb code 5dyz). 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 ASP251GLY/GLN307HIS Mutant of Cytochrome P450 BM3 in Complex with N-Palmitoylglycine, PDB code: 5dyz:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of ASP251GLY/GLN307HIS Mutant of Cytochrome P450 BM3 in Complex with N-Palmitoylglycine


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 ASP251GLY/GLN307HIS Mutant of Cytochrome P450 BM3 in Complex with N-Palmitoylglycine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:27.2 occ:1.00 FE A:HEM501 0.0 27.2 1.0 NA A:HEM501 2.0 17.1 1.0 ND A:HEM501 2.1 25.1 1.0 NB A:HEM501 2.1 27.0 1.0 NC A:HEM501 2.1 28.0 1.0 SG A:CYS400 2.3 25.1 1.0 C1A A:HEM501 3.0 23.9 1.0 C4D A:HEM501 3.1 26.5 1.0 C4A A:HEM501 3.1 22.2 1.0 C4C A:HEM501 3.1 25.2 1.0 C4B A:HEM501 3.1 17.8 1.0 C1D A:HEM501 3.1 24.9 1.0 C1B A:HEM501 3.1 22.6 1.0 C1C A:HEM501 3.1 30.2 1.0 CB A:CYS400 3.3 25.5 1.0 O A:HOH763 3.3 35.3 1.0 CHA A:HEM501 3.4 26.6 1.0 CHD A:HEM501 3.4 20.2 1.0 CHB A:HEM501 3.5 22.0 1.0 CHC A:HEM501 3.5 26.1 1.0 CA A:CYS400 4.0 22.4 1.0 C2A A:HEM501 4.3 21.8 1.0 C3A A:HEM501 4.3 20.9 1.0 C3C A:HEM501 4.3 26.4 1.0 C3B A:HEM501 4.3 25.1 1.0 C3D A:HEM501 4.3 20.9 1.0 C2B A:HEM501 4.3 25.4 1.0 C2D A:HEM501 4.3 26.9 1.0 C2C A:HEM501 4.3 28.5 1.0 CE2 A:PHE87 4.5 30.9 1.0 C A:CYS400 4.7 22.1 1.0 N A:GLY402 4.8 25.2 1.0 O A:ALA264 4.9 28.6 1.0 N A:ILE401 4.9 25.9 1.0

Iron binding site 2 out of 2 in the Crystal Structure of ASP251GLY/GLN307HIS Mutant of Cytochrome P450 BM3 in Complex with N-Palmitoylglycine


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 ASP251GLY/GLN307HIS Mutant of Cytochrome P450 BM3 in Complex with N-Palmitoylglycine within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe501 b:29.5 occ:1.00 FE C:HEM501 0.0 29.5 1.0 NB C:HEM501 1.9 22.2 1.0 ND C:HEM501 2.0 25.4 1.0 NC C:HEM501 2.1 24.2 1.0 NA C:HEM501 2.2 25.1 1.0 SG C:CYS400 2.3 27.1 1.0 C4B C:HEM501 2.9 27.0 1.0 C1B C:HEM501 3.0 26.8 1.0 C1D C:HEM501 3.0 26.7 1.0 O C:HOH686 3.0 37.0 1.0 C4D C:HEM501 3.0 30.0 1.0 C4C C:HEM501 3.1 23.0 1.0 C1C C:HEM501 3.1 23.1 1.0 C4A C:HEM501 3.1 25.9 1.0 C1A C:HEM501 3.2 22.5 1.0 CB C:CYS400 3.3 27.5 1.0 CHC C:HEM501 3.4 27.6 1.0 CHD C:HEM501 3.4 22.8 1.0 CHB C:HEM501 3.5 26.9 1.0 CHA C:HEM501 3.5 21.8 1.0 CA C:CYS400 4.0 28.4 1.0 C3B C:HEM501 4.2 19.7 1.0 C2B C:HEM501 4.2 23.8 1.0 C3D C:HEM501 4.2 21.9 1.0 C2D C:HEM501 4.3 25.1 1.0 C3C C:HEM501 4.3 16.9 1.0 C2C C:HEM501 4.3 20.8 1.0 C3A C:HEM501 4.4 22.5 1.0 C2A C:HEM501 4.4 21.6 1.0 CE2 C:PHE87 4.6 33.8 1.0 O C:ALA264 4.6 22.9 1.0 C C:CYS400 4.8 30.1 1.0 N C:GLY402 4.8 29.5 1.0 N C:ILE401 4.9 29.9 1.0

G.Di Nardo, V.Dell'angelo, G.Catucci, S.J.Sadeghi, G.Gilardi. Subtle Structural Changes in the ASP251GLY/GLN307HIS P450 BM3 Mutant Responsible For New Activity Toward Diclofenac, Tolbutamide and Ibuprofen. Arch.Biochem.Biophys. V. 602 106 2016.
ISSN: ESSN 1096-0384
PubMed: 26718083
DOI: 10.1016/J.ABB.2015.12.005