Iron in PDB 6f8a: Crystal Structure of Cytochrome P450 CYP260A1 (S276I) Bound with Histidine

The structure of Crystal Structure of Cytochrome P450 CYP260A1 (S276I) Bound with Histidine, PDB code: 6f8a was solved by I.K.Jozwik, A.M.W.H.Thunnissen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.65 / 1.35
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	101.221, 65.151, 128.533, 90.00, 112.81, 90.00
R / Rfree (%)	17.8 / 19.4

The binding sites of Iron atom in the Crystal Structure of Cytochrome P450 CYP260A1 (S276I) Bound with Histidine (pdb code 6f8a). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of Cytochrome P450 CYP260A1 (S276I) Bound with Histidine, PDB code: 6f8a:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Crystal Structure of Cytochrome P450 CYP260A1 (S276I) Bound with Histidine


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 Cytochrome P450 CYP260A1 (S276I) Bound with Histidine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:10.7 occ:0.60 FE A:HEM501 0.0 10.7 0.6 FE A:HEM501 0.3 5.6 0.4 NC A:HEM501 1.8 9.3 0.4 NC A:HEM501 2.0 9.3 0.6 NB A:HEM501 2.0 8.5 0.6 NB A:HEM501 2.0 9.7 0.4 ND A:HEM501 2.0 9.4 0.6 NA A:HEM501 2.1 9.8 0.6 ND A:HEM501 2.1 10.5 0.4 NE2 A:HIS502 2.2 14.7 1.0 SG A:CYS340 2.2 9.9 1.0 NA A:HEM501 2.3 9.8 0.4 C1C A:HEM501 2.8 9.9 0.4 C4C A:HEM501 2.9 9.2 0.4 C4B A:HEM501 2.9 9.3 0.4 C4B A:HEM501 3.0 9.3 0.6 C1C A:HEM501 3.0 9.7 0.6 C4C A:HEM501 3.0 7.6 0.6 C1B A:HEM501 3.0 8.8 0.6 C1D A:HEM501 3.0 7.2 0.6 C1D A:HEM501 3.0 9.8 0.4 C4A A:HEM501 3.1 10.2 0.6 C4D A:HEM501 3.1 8.2 0.6 C1A A:HEM501 3.1 9.2 0.6 C1B A:HEM501 3.1 7.6 0.4 CE1 A:HIS502 3.1 14.7 1.0 C4D A:HEM501 3.2 9.6 0.4 CHC A:HEM501 3.2 9.3 0.4 CD2 A:HIS502 3.2 14.7 1.0 C1A A:HEM501 3.3 8.8 0.4 C4A A:HEM501 3.3 7.2 0.4 CHD A:HEM501 3.3 10.6 0.4 CHC A:HEM501 3.4 9.5 0.6 CB A:CYS340 3.4 8.7 1.0 CHD A:HEM501 3.4 8.7 0.6 CHB A:HEM501 3.4 9.2 0.6 CHA A:HEM501 3.5 9.5 0.6 CHA A:HEM501 3.6 9.7 0.4 CHB A:HEM501 3.6 8.8 0.4 C2C A:HEM501 4.0 10.9 0.4 C3C A:HEM501 4.0 10.8 0.4 C3B A:HEM501 4.2 10.1 0.4 C3B A:HEM501 4.2 10.3 0.6 C2B A:HEM501 4.2 11.2 0.6 C2C A:HEM501 4.2 9.7 0.6 C3C A:HEM501 4.2 8.8 0.6 C2D A:HEM501 4.3 8.7 0.6 ND1 A:HIS502 4.3 14.7 1.0 CA A:CYS340 4.3 8.7 1.0 C2B A:HEM501 4.3 8.9 0.4 C3D A:HEM501 4.3 8.8 0.6 C2D A:HEM501 4.3 10.2 0.4 C3A A:HEM501 4.3 10.2 0.6 C2A A:HEM501 4.3 10.2 0.6 CG A:HIS502 4.3 14.7 1.0 C3D A:HEM501 4.4 10.5 0.4 C2A A:HEM501 4.5 8.5 0.4 C3A A:HEM501 4.5 8.6 0.4 N A:GLY342 4.8 11.5 1.0 C A:CYS340 5.0 9.7 1.0

Iron binding site 2 out of 4 in the Crystal Structure of Cytochrome P450 CYP260A1 (S276I) Bound with Histidine


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 Cytochrome P450 CYP260A1 (S276I) Bound with Histidine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:5.6 occ:0.40 FE A:HEM501 0.0 5.6 0.4 FE A:HEM501 0.3 10.7 0.6 ND A:HEM501 1.7 9.4 0.6 NA A:HEM501 2.0 9.8 0.6 NA A:HEM501 2.0 9.8 0.4 ND A:HEM501 2.0 10.5 0.4 NE2 A:HIS502 2.0 14.7 1.0 NB A:HEM501 2.1 9.7 0.4 NC A:HEM501 2.1 9.3 0.4 NC A:HEM501 2.1 9.3 0.6 NB A:HEM501 2.3 8.5 0.6 SG A:CYS340 2.4 9.9 1.0 C4D A:HEM501 2.8 8.2 0.6 C1D A:HEM501 2.8 7.2 0.6 C1A A:HEM501 2.9 9.2 0.6 CE1 A:HIS502 2.9 14.7 1.0 C1A A:HEM501 3.0 8.8 0.4 C4D A:HEM501 3.0 9.6 0.4 C4C A:HEM501 3.0 7.6 0.6 C1D A:HEM501 3.0 9.8 0.4 C4A A:HEM501 3.0 7.2 0.4 C4B A:HEM501 3.1 9.3 0.4 C4C A:HEM501 3.1 9.2 0.4 C1C A:HEM501 3.1 9.9 0.4 C4A A:HEM501 3.1 10.2 0.6 C1B A:HEM501 3.1 7.6 0.4 CD2 A:HIS502 3.1 14.7 1.0 C1C A:HEM501 3.2 9.7 0.6 CHA A:HEM501 3.2 9.5 0.6 C1B A:HEM501 3.2 8.8 0.6 CHD A:HEM501 3.3 8.7 0.6 C4B A:HEM501 3.3 9.3 0.6 CHA A:HEM501 3.3 9.7 0.4 CB A:CYS340 3.4 8.7 1.0 CHD A:HEM501 3.4 10.6 0.4 CHC A:HEM501 3.4 9.3 0.4 CHB A:HEM501 3.5 8.8 0.4 CHB A:HEM501 3.5 9.2 0.6 CHC A:HEM501 3.6 9.5 0.6 C3D A:HEM501 4.0 8.8 0.6 C2D A:HEM501 4.0 8.7 0.6 ND1 A:HIS502 4.1 14.7 1.0 CG A:HIS502 4.2 14.7 1.0 C2A A:HEM501 4.2 10.2 0.6 C2A A:HEM501 4.2 8.5 0.4 C3D A:HEM501 4.2 10.5 0.4 C2D A:HEM501 4.2 10.2 0.4 C3A A:HEM501 4.2 8.6 0.4 C3A A:HEM501 4.2 10.2 0.6 CA A:CYS340 4.3 8.7 1.0 C3C A:HEM501 4.3 10.8 0.4 C3C A:HEM501 4.3 8.8 0.6 C3B A:HEM501 4.3 10.1 0.4 C2C A:HEM501 4.3 10.9 0.4 C2B A:HEM501 4.3 8.9 0.4 C2C A:HEM501 4.4 9.7 0.6 C2B A:HEM501 4.5 11.2 0.6 C3B A:HEM501 4.5 10.3 0.6

Iron binding site 3 out of 4 in the Crystal Structure of Cytochrome P450 CYP260A1 (S276I) Bound with Histidine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of Cytochrome P450 CYP260A1 (S276I) Bound with Histidine within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:11.5 occ:0.70 FE B:HEM501 0.0 11.5 0.7 FE B:HEM501 0.4 7.8 0.3 NA B:HEM501 1.8 10.8 0.3 ND B:HEM501 1.9 10.5 0.7 NB B:HEM501 2.0 10.1 0.3 NA B:HEM501 2.0 10.7 0.7 NC B:HEM501 2.0 10.0 0.7 ND B:HEM501 2.1 10.6 0.3 NE2 B:HIS502 2.1 14.7 1.0 NB B:HEM501 2.1 11.2 0.7 NC B:HEM501 2.2 10.8 0.3 SG B:CYS340 2.3 11.3 1.0 C4A B:HEM501 2.8 9.7 0.3 C1A B:HEM501 2.9 9.9 0.3 C1D B:HEM501 2.9 9.9 0.7 C4D B:HEM501 2.9 9.4 0.7 C1B B:HEM501 2.9 9.8 0.3 CE1 B:HIS502 2.9 15.3 1.0 C1A B:HEM501 3.0 8.8 0.7 C4C B:HEM501 3.0 9.7 0.7 C4D B:HEM501 3.0 9.3 0.3 C4B B:HEM501 3.1 10.3 0.3 C1C B:HEM501 3.1 10.4 0.7 C4A B:HEM501 3.1 11.6 0.7 C4B B:HEM501 3.1 10.4 0.7 C1D B:HEM501 3.1 11.9 0.3 C1B B:HEM501 3.2 10.3 0.7 C1C B:HEM501 3.2 10.9 0.3 C4C B:HEM501 3.2 10.7 0.3 CD2 B:HIS502 3.2 14.9 1.0 CHB B:HEM501 3.2 10.3 0.3 CHA B:HEM501 3.3 9.6 0.7 CHD B:HEM501 3.3 10.3 0.7 CHA B:HEM501 3.3 9.6 0.3 CB B:CYS340 3.4 8.9 1.0 CHC B:HEM501 3.5 10.7 0.7 CHB B:HEM501 3.5 10.7 0.7 CHC B:HEM501 3.5 11.0 0.3 CHD B:HEM501 3.5 11.0 0.3 C3A B:HEM501 4.1 10.6 0.3 C2A B:HEM501 4.1 11.4 0.3 C2D B:HEM501 4.1 10.6 0.7 C3D B:HEM501 4.1 11.8 0.7 ND1 B:HIS502 4.1 15.1 1.0 C2B B:HEM501 4.2 10.4 0.3 CA B:CYS340 4.2 9.7 1.0 C2A B:HEM501 4.2 10.7 0.7 C3B B:HEM501 4.2 9.8 0.3 C3A B:HEM501 4.3 10.1 0.7 C3C B:HEM501 4.3 10.2 0.7 C3D B:HEM501 4.3 10.9 0.3 CG B:HIS502 4.3 16.2 1.0 C2C B:HEM501 4.3 9.3 0.7 C2D B:HEM501 4.3 10.6 0.3 C3B B:HEM501 4.3 11.4 0.7 C2B B:HEM501 4.4 11.7 0.7 C2C B:HEM501 4.4 11.9 0.3 C3C B:HEM501 4.4 11.9 0.3 C B:CYS340 5.0 10.7 1.0 N B:GLY342 5.0 11.0 1.0

Iron binding site 4 out of 4 in the Crystal Structure of Cytochrome P450 CYP260A1 (S276I) Bound with Histidine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of Cytochrome P450 CYP260A1 (S276I) Bound with Histidine within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:7.8 occ:0.30 FE B:HEM501 0.0 7.8 0.3 FE B:HEM501 0.4 11.5 0.7 NB B:HEM501 1.8 11.2 0.7 NC B:HEM501 1.9 10.8 0.3 NB B:HEM501 2.0 10.1 0.3 NA B:HEM501 2.0 10.7 0.7 NC B:HEM501 2.0 10.0 0.7 ND B:HEM501 2.1 10.6 0.3 NA B:HEM501 2.2 10.8 0.3 NE2 B:HIS502 2.2 14.7 1.0 SG B:CYS340 2.2 11.3 1.0 ND B:HEM501 2.3 10.5 0.7 C4B B:HEM501 2.8 10.4 0.7 C1B B:HEM501 2.8 10.3 0.7 C1C B:HEM501 2.9 10.9 0.3 C4C B:HEM501 2.9 10.7 0.3 C4B B:HEM501 2.9 10.3 0.3 C1C B:HEM501 2.9 10.4 0.7 C4A B:HEM501 2.9 11.6 0.7 C1D B:HEM501 3.0 11.9 0.3 C1B B:HEM501 3.1 9.8 0.3 C1A B:HEM501 3.1 8.8 0.7 CE1 B:HIS502 3.1 15.3 1.0 C4D B:HEM501 3.2 9.3 0.3 C4C B:HEM501 3.2 9.7 0.7 C4A B:HEM501 3.2 9.7 0.3 CHC B:HEM501 3.2 10.7 0.7 CHC B:HEM501 3.2 11.0 0.3 CHB B:HEM501 3.3 10.7 0.7 C1A B:HEM501 3.3 9.9 0.3 CD2 B:HIS502 3.3 14.9 1.0 C4D B:HEM501 3.3 9.4 0.7 C1D B:HEM501 3.3 9.9 0.7 CHD B:HEM501 3.3 11.0 0.3 CB B:CYS340 3.5 8.9 1.0 CHB B:HEM501 3.5 10.3 0.3 CHA B:HEM501 3.6 9.6 0.7 CHA B:HEM501 3.6 9.6 0.3 CHD B:HEM501 3.6 10.3 0.7 C3B B:HEM501 4.0 11.4 0.7 C2B B:HEM501 4.0 11.7 0.7 C2C B:HEM501 4.1 11.9 0.3 C3C B:HEM501 4.1 11.9 0.3 C3B B:HEM501 4.2 9.8 0.3 C3A B:HEM501 4.2 10.1 0.7 C2C B:HEM501 4.2 9.3 0.7 C2B B:HEM501 4.3 10.4 0.3 C2D B:HEM501 4.3 10.6 0.3 C2A B:HEM501 4.3 10.7 0.7 ND1 B:HIS502 4.3 15.1 1.0 CA B:CYS340 4.3 9.7 1.0 C3D B:HEM501 4.3 10.9 0.3 C3C B:HEM501 4.3 10.2 0.7 CG B:HIS502 4.4 16.2 1.0 C3A B:HEM501 4.4 10.6 0.3 C2A B:HEM501 4.5 11.4 0.3 C2D B:HEM501 4.5 10.6 0.7 C3D B:HEM501 4.5 11.8 0.7 N B:GLY342 4.7 11.0 1.0 C B:CYS340 4.9 10.7 1.0

Y.Khatri, I.K.Jozwik, M.Ringle, I.A.Ionescu, M.Litzenburger, M.C.Hutter, A.W.H.Thunnissen, R.Bernhardt. Structure-Based Engineering of Steroidogenic CYP260A1 For Stereo- and Regioselective Hydroxylation of Progesterone. Acs Chem. Biol. V. 13 1021 2018.
ISSN: ESSN 1554-8937
PubMed: 29509407
DOI: 10.1021/ACSCHEMBIO.8B00026