Iron in PDB 5x7e: Crystal Structure of Vitamin D Hydroxylase Cytochrome P450 105A1 (R84A Mutant) in Complex with 1,25-Dihydroxyvitamin D2

The structure of Crystal Structure of Vitamin D Hydroxylase Cytochrome P450 105A1 (R84A Mutant) in Complex with 1,25-Dihydroxyvitamin D2, PDB code: 5x7e was solved by K.Hayashi, K.Yasuda, Y.Shiro, H.Sugimoto, T.Sakaki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	17.53 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	52.409, 53.360, 139.436, 90.00, 90.00, 90.00
R / Rfree (%)	18.6 / 23.2

The binding sites of Iron atom in the Crystal Structure of Vitamin D Hydroxylase Cytochrome P450 105A1 (R84A Mutant) in Complex with 1,25-Dihydroxyvitamin D2 (pdb code 5x7e). 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 Crystal Structure of Vitamin D Hydroxylase Cytochrome P450 105A1 (R84A Mutant) in Complex with 1,25-Dihydroxyvitamin D2, PDB code: 5x7e:

Iron binding site 1 out of 1 in the Crystal Structure of Vitamin D Hydroxylase Cytochrome P450 105A1 (R84A Mutant) in Complex with 1,25-Dihydroxyvitamin D2


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 Vitamin D Hydroxylase Cytochrome P450 105A1 (R84A Mutant) in Complex with 1,25-Dihydroxyvitamin D2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:10.7 occ:1.00 FE A:HEM501 0.0 10.7 1.0 ND A:HEM501 2.0 10.3 1.0 NB A:HEM501 2.0 9.7 1.0 NC A:HEM501 2.1 10.2 1.0 NA A:HEM501 2.1 10.0 1.0 SG A:CYS355 2.4 10.9 1.0 C4B A:HEM501 3.0 9.9 1.0 C1D A:HEM501 3.0 11.0 1.0 C1C A:HEM501 3.1 11.2 1.0 C4D A:HEM501 3.1 10.5 1.0 C4C A:HEM501 3.1 11.0 1.0 C1B A:HEM501 3.1 9.4 1.0 C1A A:HEM501 3.1 9.9 1.0 C4A A:HEM501 3.1 9.8 1.0 CB A:CYS355 3.3 10.1 1.0 CHC A:HEM501 3.4 10.4 1.0 CHD A:HEM501 3.4 10.7 1.0 CHA A:HEM501 3.4 10.6 1.0 CHB A:HEM501 3.5 9.2 1.0 CA A:CYS355 3.9 11.1 1.0 C3B A:HEM501 4.3 10.0 1.0 C2B A:HEM501 4.3 9.3 1.0 C2D A:HEM501 4.3 10.9 1.0 C3C A:HEM501 4.3 11.6 1.0 C2C A:HEM501 4.3 10.9 1.0 C3D A:HEM501 4.3 11.4 1.0 C2A A:HEM501 4.3 10.1 1.0 C3A A:HEM501 4.4 9.7 1.0 O A:HOH875 4.5 46.9 1.0 C A:CYS355 4.7 11.4 1.0 N A:GLY357 4.7 10.2 1.0 N A:LEU356 4.7 11.2 1.0 CD1 A:PHE348 4.9 9.8 1.0 CG2 A:THR248 4.9 14.4 1.0

K.Yasuda, Y.Yogo, H.Sugimoto, H.Mano, T.Takita, M.Ohta, M.Kamakura, S.Ikushiro, K.Yasukawa, Y.Shiro, T.Sakaki. Production of An Active Form of Vitamin D2 By Genetically Engineered CYP105A1 Biochem. Biophys. Res. V. 486 336 2017COMMUN..
ISSN: ESSN 1090-2104
PubMed: 28302483
DOI: 10.1016/J.BBRC.2017.03.040