Iron in PDB 5gnl: Cytochrome P450 Vdh (CYP107BR1) F106V Mutant

All present enzymatic activity of Cytochrome P450 Vdh (CYP107BR1) F106V Mutant:
1.14.15.15;

The structure of Cytochrome P450 Vdh (CYP107BR1) F106V Mutant, PDB code: 5gnl was solved by Y.Yasutake, T.Tamura, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.95
Space group	P 31
Cell size a, b, c (Å), α, β, γ (°)	61.670, 61.670, 98.166, 90.00, 90.00, 120.00
R / Rfree (%)	20 / 23.4

The binding sites of Iron atom in the Cytochrome P450 Vdh (CYP107BR1) F106V Mutant (pdb code 5gnl). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Cytochrome P450 Vdh (CYP107BR1) F106V Mutant, PDB code: 5gnl:

Iron binding site 1 out of 1 in the Cytochrome P450 Vdh (CYP107BR1) F106V Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome P450 Vdh (CYP107BR1) F106V Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:29.6 occ:1.00 FE A:HEM501 0.0 29.6 1.0 ND A:HEM501 1.9 29.1 1.0 NA A:HEM501 2.0 27.9 1.0 NB A:HEM501 2.1 26.9 1.0 NC A:HEM501 2.1 28.5 1.0 O A:HOH665 2.4 41.0 1.0 SG A:CYS347 2.5 30.3 1.0 C1D A:HEM501 2.9 29.1 1.0 C4D A:HEM501 2.9 27.2 1.0 C1A A:HEM501 3.0 27.8 1.0 C4B A:HEM501 3.0 27.8 1.0 C4A A:HEM501 3.1 27.9 1.0 C1B A:HEM501 3.1 28.1 1.0 C4C A:HEM501 3.1 29.9 1.0 C1C A:HEM501 3.1 28.7 1.0 CHD A:HEM501 3.4 28.6 1.0 CHA A:HEM501 3.4 27.2 1.0 CB A:CYS347 3.4 27.7 1.0 CHB A:HEM501 3.4 26.9 1.0 CHC A:HEM501 3.5 27.8 1.0 CA A:CYS347 4.0 27.5 1.0 O A:ALA236 4.2 31.6 1.0 C2D A:HEM501 4.2 28.2 1.0 C3D A:HEM501 4.2 26.8 1.0 C2A A:HEM501 4.3 28.5 1.0 C3A A:HEM501 4.3 28.1 1.0 C2B A:HEM501 4.3 26.8 1.0 C3B A:HEM501 4.3 28.3 1.0 C3C A:HEM501 4.3 31.2 1.0 C2C A:HEM501 4.3 29.2 1.0 CB A:ALA236 4.5 30.4 1.0 N A:LEU348 4.7 28.5 1.0 C A:CYS347 4.7 27.9 1.0 N A:GLY349 4.7 30.5 1.0 OTT A:PG0502 4.7 44.9 1.0 C A:ALA236 4.8 31.6 1.0

Y.Yasutake, T.Kameda, T.Tamura. Structural Insights Into the Mechanism of the Drastic Changes in Enzymatic Activity of the Cytochrome P450 Vitamin D3 Hydroxylase (CYP107BR1) Caused By A Mutation Distant From the Active Site Acta Crystallogr F Struct V. 73 266 2017BIOL Commun.
ISSN: ESSN 2053-230X
PubMed: 28471358
DOI: 10.1107/S2053230X17004782