Iron in PDB 5dyp: Crystal Structure of ASP251GLY/GLN307HIS Mutant of Cytochrome P450 BM3

All present enzymatic activity of Crystal Structure of ASP251GLY/GLN307HIS Mutant of Cytochrome P450 BM3:
1.14.14.1; 1.6.2.4;

The structure of Crystal Structure of ASP251GLY/GLN307HIS Mutant of Cytochrome P450 BM3, PDB code: 5dyp 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)	47.00 / 2.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	61.134, 118.448, 146.947, 90.00, 90.00, 90.00
R / Rfree (%)	22 / 25.7

The binding sites of Iron atom in the Crystal Structure of ASP251GLY/GLN307HIS Mutant of Cytochrome P450 BM3 (pdb code 5dyp). 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, PDB code: 5dyp:
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


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:88.5 occ:1.00 FE A:HEM501 0.0 88.5 1.0 NC A:HEM501 2.0 41.0 1.0 NB A:HEM501 2.0 52.8 1.0 NA A:HEM501 2.1 57.9 1.0 ND A:HEM501 2.1 46.7 1.0 SG A:CYS400 2.3 47.9 1.0 O A:HOH670 2.9 30.0 1.0 C1C A:HEM501 3.1 44.6 1.0 C4C A:HEM501 3.1 27.5 1.0 C4B A:HEM501 3.1 42.1 1.0 C1B A:HEM501 3.1 30.9 1.0 C4A A:HEM501 3.1 44.4 1.0 C1A A:HEM501 3.1 35.9 1.0 C1D A:HEM501 3.1 29.5 1.0 C4D A:HEM501 3.1 43.6 1.0 CB A:CYS400 3.2 39.9 1.0 CHC A:HEM501 3.4 45.4 1.0 CHD A:HEM501 3.4 27.0 1.0 CHB A:HEM501 3.4 42.5 1.0 CHA A:HEM501 3.5 37.4 1.0 CA A:CYS400 3.9 41.9 1.0 C2C A:HEM501 4.3 44.9 1.0 C3C A:HEM501 4.3 47.7 1.0 C3B A:HEM501 4.3 28.9 1.0 C2B A:HEM501 4.3 45.6 1.0 C3A A:HEM501 4.3 49.2 1.0 C2A A:HEM501 4.3 47.9 1.0 C2D A:HEM501 4.3 42.2 1.0 C3D A:HEM501 4.3 36.7 1.0 CE2 A:PHE87 4.7 58.3 1.0 C A:CYS400 4.7 63.0 1.0 O A:ALA264 4.8 52.4 1.0 N A:GLY402 4.8 43.8 1.0 N A:ILE401 4.9 55.7 1.0 CB A:ALA264 5.0 45.7 1.0

Iron binding site 2 out of 2 in the Crystal Structure of ASP251GLY/GLN307HIS 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 Crystal Structure of ASP251GLY/GLN307HIS Mutant of Cytochrome P450 BM3 within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe501 b:57.2 occ:1.00 FE C:HEM501 0.0 57.2 1.0 NC C:HEM501 2.0 60.4 1.0 NB C:HEM501 2.1 48.7 1.0 NA C:HEM501 2.1 48.5 1.0 ND C:HEM501 2.1 30.8 1.0 SG C:CYS400 2.3 87.0 1.0 O C:HOH640 2.8 30.0 1.0 C4C C:HEM501 3.0 48.5 1.0 C1C C:HEM501 3.1 56.4 1.0 C4B C:HEM501 3.1 56.0 1.0 C1D C:HEM501 3.1 41.8 1.0 C1B C:HEM501 3.1 41.3 1.0 C4A C:HEM501 3.1 30.4 1.0 C1A C:HEM501 3.1 29.2 1.0 C4D C:HEM501 3.1 46.1 1.0 CB C:CYS400 3.2 56.5 1.0 CHD C:HEM501 3.4 50.7 1.0 CHC C:HEM501 3.4 55.2 1.0 CHA C:HEM501 3.5 41.4 1.0 CHB C:HEM501 3.5 45.2 1.0 CA C:CYS400 4.1 52.8 1.0 C3C C:HEM501 4.3 53.7 1.0 C2C C:HEM501 4.3 58.0 1.0 C3B C:HEM501 4.3 42.0 1.0 C2B C:HEM501 4.3 44.3 1.0 C3A C:HEM501 4.3 39.6 1.0 C2A C:HEM501 4.3 39.8 1.0 C2D C:HEM501 4.3 35.2 1.0 C3D C:HEM501 4.3 48.5 1.0 CE2 C:PHE87 4.7 50.3 1.0 O C:ALA264 4.7 56.8 1.0 C C:CYS400 4.9 54.5 1.0 CD1 C:PHE393 5.0 59.1 1.0 OG1 C:THR268 5.0 55.6 1.0 N C:GLY402 5.0 64.4 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