Iron in PDB 4yt3: CYP106A2

All present enzymatic activity of CYP106A2:
1.14.15.8;

The structure of CYP106A2, PDB code: 4yt3 was solved by S.Janocha, Y.Carius, R.Bernhardt, C.R.D.Lancaster, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	66.18 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	47.060, 114.060, 83.450, 90.00, 103.14, 90.00
R / Rfree (%)	16.3 / 19.9

The binding sites of Iron atom in the CYP106A2 (pdb code 4yt3). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the CYP106A2, PDB code: 4yt3:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the CYP106A2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of CYP106A2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:10.6 occ:1.00 FE A:HEM501 0.0 10.6 1.0 ND A:HEM501 2.0 9.4 1.0 NA A:HEM501 2.0 10.1 1.0 NB A:HEM501 2.0 8.8 1.0 NC A:HEM501 2.1 10.2 1.0 SG A:CYS355 2.3 12.1 1.0 O A:HOH822 2.4 23.3 1.0 C1D A:HEM501 2.9 9.7 1.0 C4B A:HEM501 3.0 10.7 1.0 C1A A:HEM501 3.0 9.9 1.0 C4D A:HEM501 3.0 10.2 1.0 C1C A:HEM501 3.0 10.9 1.0 C1B A:HEM501 3.0 9.1 1.0 C4A A:HEM501 3.1 10.4 1.0 C4C A:HEM501 3.1 10.8 1.0 CHC A:HEM501 3.4 10.4 1.0 CB A:CYS355 3.4 8.6 1.0 CHA A:HEM501 3.4 10.4 1.0 CHB A:HEM501 3.4 9.1 1.0 CHD A:HEM501 3.4 9.3 1.0 CA A:CYS355 4.1 9.0 1.0 C2D A:HEM501 4.2 10.9 1.0 C3D A:HEM501 4.2 10.7 1.0 C2B A:HEM501 4.2 10.0 1.0 C2C A:HEM501 4.2 11.3 1.0 C3B A:HEM501 4.3 9.7 1.0 C3A A:HEM501 4.3 10.1 1.0 C2A A:HEM501 4.3 9.7 1.0 O A:ALA243 4.3 17.5 1.0 C3C A:HEM501 4.3 11.7 1.0 N A:GLY357 4.6 11.2 1.0 C A:CYS355 4.8 9.4 1.0 N A:LEU356 4.8 9.3 1.0 CB A:ALA243 4.9 16.6 1.0 CA A:GLY357 4.9 11.7 1.0

Iron binding site 2 out of 2 in the CYP106A2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of CYP106A2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:10.6 occ:1.00 FE B:HEM501 0.0 10.6 1.0 ND B:HEM501 1.9 10.1 1.0 NB B:HEM501 2.0 11.5 1.0 NA B:HEM501 2.1 11.4 1.0 NC B:HEM501 2.1 10.7 1.0 O B:HOH808 2.3 24.7 1.0 SG B:CYS355 2.4 12.8 1.0 C1D B:HEM501 2.9 10.2 1.0 C1B B:HEM501 3.0 12.0 1.0 C4D B:HEM501 3.0 10.7 1.0 C1A B:HEM501 3.1 9.9 1.0 C4B B:HEM501 3.1 11.4 1.0 C4C B:HEM501 3.1 11.7 1.0 C1C B:HEM501 3.1 10.4 1.0 C4A B:HEM501 3.1 10.4 1.0 CB B:CYS355 3.4 11.3 1.0 CHD B:HEM501 3.4 10.5 1.0 CHB B:HEM501 3.5 10.7 1.0 CHC B:HEM501 3.5 10.9 1.0 CHA B:HEM501 3.5 10.9 1.0 CA B:CYS355 4.0 10.4 1.0 C2B B:HEM501 4.2 11.7 1.0 C2D B:HEM501 4.2 11.4 1.0 C3B B:HEM501 4.2 11.1 1.0 C3C B:HEM501 4.3 12.8 1.0 C2C B:HEM501 4.3 11.2 1.0 C2A B:HEM501 4.3 9.5 1.0 C3D B:HEM501 4.3 10.9 1.0 C3A B:HEM501 4.3 10.0 1.0 O B:ALA243 4.3 18.1 1.0 N B:GLY357 4.6 10.2 1.0 C B:CYS355 4.7 10.6 1.0 N B:LEU356 4.8 11.4 1.0 CB B:ALA243 4.9 19.0 1.0 CA B:GLY357 4.9 9.5 1.0

S.Janocha, Y.Carius, M.Hutter, C.R.Lancaster, R.Bernhardt. Crystal Structure of CYP106A2 in Substrate-Free and Substrate-Bound Form. Chembiochem V. 17 852 2016.
ISSN: ESSN 1439-7633
PubMed: 26864272
DOI: 10.1002/CBIC.201500524