Iron in PDB 7tto: P450 (Oxya) From Kistamicin Biosynthesis, Mixed Heme Conformation

The structure of P450 (Oxya) From Kistamicin Biosynthesis, Mixed Heme Conformation, PDB code: 7tto was solved by A.Greule, T.Izore, M.J.Cryle, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.70 / 1.60
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	69.996, 69.996, 132.386, 90, 90, 120
R / Rfree (%)	19.8 / 22.4

The binding sites of Iron atom in the P450 (Oxya) From Kistamicin Biosynthesis, Mixed Heme Conformation (pdb code 7tto). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the P450 (Oxya) From Kistamicin Biosynthesis, Mixed Heme Conformation, PDB code: 7tto:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the P450 (Oxya) From Kistamicin Biosynthesis, Mixed Heme Conformation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of P450 (Oxya) From Kistamicin Biosynthesis, Mixed Heme Conformation within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:11.0 occ:0.62 FE A:HEM401 0.0 11.0 0.6 FE A:HEM401 0.6 16.8 0.4 NB A:HEM401 1.9 16.0 0.4 NC A:HEM401 1.9 14.8 0.4 NB A:HEM401 1.9 14.7 0.6 ND A:HEM401 1.9 15.9 0.6 ND A:HEM401 2.0 17.0 0.4 NA A:HEM401 2.0 17.1 0.6 NC A:HEM401 2.0 14.2 0.6 NA A:HEM401 2.0 15.1 0.4 SG A:CYS332 2.0 15.3 1.0 O A:HOH507 2.4 20.4 1.0 C4B A:HEM401 3.0 14.6 0.4 C4D A:HEM401 3.0 14.4 0.6 C1B A:HEM401 3.0 14.3 0.4 C4B A:HEM401 3.0 16.5 0.6 C1C A:HEM401 3.0 16.4 0.4 C4C A:HEM401 3.0 16.0 0.4 C4A A:HEM401 3.0 13.9 0.4 C4D A:HEM401 3.0 17.3 0.4 C1B A:HEM401 3.0 16.5 0.6 C4A A:HEM401 3.1 14.5 0.6 C1D A:HEM401 3.1 13.5 0.6 C4C A:HEM401 3.1 12.4 0.6 C1A A:HEM401 3.1 17.2 0.6 C1D A:HEM401 3.1 14.5 0.4 C1C A:HEM401 3.1 13.9 0.6 C1A A:HEM401 3.1 13.9 0.4 HB2 A:CYS332 3.2 15.9 1.0 CB A:CYS332 3.2 13.2 1.0 HA A:CYS332 3.5 17.5 1.0 CHA A:HEM401 3.6 13.2 0.6 CHC A:HEM401 3.7 17.2 0.4 CHB A:HEM401 3.7 13.2 0.4 CHC A:HEM401 3.7 18.6 0.6 CHA A:HEM401 3.7 15.5 0.4 CHD A:HEM401 3.7 17.6 0.4 CHB A:HEM401 3.7 18.9 0.6 CHD A:HEM401 3.7 14.7 0.6 H A:GLY334 3.8 17.6 1.0 CA A:CYS332 3.9 14.6 1.0 OE1 A:GLN228 4.0 31.9 1.0 HB3 A:CYS332 4.0 15.9 1.0 HD1 A:PHE325 4.2 17.7 1.0 C3B A:HEM401 4.2 17.2 0.4 C2B A:HEM401 4.2 16.1 0.4 C2C A:HEM401 4.3 15.0 0.4 C3C A:HEM401 4.3 10.8 0.4 C3D A:HEM401 4.3 13.8 0.6 C3B A:HEM401 4.3 19.3 0.6 C2B A:HEM401 4.3 18.9 0.6 C3A A:HEM401 4.3 8.2 0.4 C2D A:HEM401 4.3 14.1 0.6 C3D A:HEM401 4.3 15.6 0.4 C2A A:HEM401 4.3 14.6 0.6 C2D A:HEM401 4.3 15.7 0.4 C2A A:HEM401 4.3 11.6 0.4 C3C A:HEM401 4.3 9.0 0.6 C3A A:HEM401 4.3 12.9 0.6 C2C A:HEM401 4.3 10.3 0.6 O A:HOH698 4.4 36.9 1.0 H A:LEU333 4.4 18.1 1.0 HHA A:HEM401 4.5 15.8 0.6 C A:CYS332 4.6 12.9 1.0 HHC A:HEM401 4.6 20.6 0.4 HHB A:HEM401 4.6 15.8 0.4 HHC A:HEM401 4.6 22.4 0.6 N A:GLY334 4.6 14.7 1.0 HHA A:HEM401 4.6 18.6 0.4 HHD A:HEM401 4.7 21.2 0.4 HHB A:HEM401 4.7 22.7 0.6 HHD A:HEM401 4.7 17.6 0.6 HA3 A:GLY334 4.7 19.2 1.0 N A:LEU333 4.7 15.1 1.0 HD2 A:PHE271 5.0 19.9 1.0

Iron binding site 2 out of 2 in the P450 (Oxya) From Kistamicin Biosynthesis, Mixed Heme Conformation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of P450 (Oxya) From Kistamicin Biosynthesis, Mixed Heme Conformation within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:16.8 occ:0.38 FE A:HEM401 0.0 16.8 0.4 FE A:HEM401 0.6 11.0 0.6 O A:HOH507 1.8 20.4 1.0 ND A:HEM401 1.9 15.9 0.6 NB A:HEM401 1.9 16.0 0.4 NA A:HEM401 1.9 17.1 0.6 ND A:HEM401 1.9 17.0 0.4 NB A:HEM401 1.9 14.7 0.6 NC A:HEM401 2.0 14.2 0.6 NA A:HEM401 2.0 15.1 0.4 NC A:HEM401 2.0 14.8 0.4 SG A:CYS332 2.6 15.3 1.0 C4D A:HEM401 3.0 14.4 0.6 C4D A:HEM401 3.0 17.3 0.4 C1D A:HEM401 3.0 13.5 0.6 C4B A:HEM401 3.0 14.6 0.4 C4A A:HEM401 3.0 14.5 0.6 C4C A:HEM401 3.0 12.4 0.6 C1B A:HEM401 3.0 14.3 0.4 C4A A:HEM401 3.0 13.9 0.4 C1B A:HEM401 3.0 16.5 0.6 C1A A:HEM401 3.0 17.2 0.6 C4B A:HEM401 3.0 16.5 0.6 C1C A:HEM401 3.1 16.4 0.4 C4C A:HEM401 3.1 16.0 0.4 C1A A:HEM401 3.1 13.9 0.4 C1D A:HEM401 3.1 14.5 0.4 C1C A:HEM401 3.1 13.9 0.6 OE1 A:GLN228 3.5 31.9 1.0 HB2 A:CYS332 3.6 15.9 1.0 CHA A:HEM401 3.6 13.2 0.6 CHA A:HEM401 3.7 15.5 0.4 CHC A:HEM401 3.7 17.2 0.4 CHD A:HEM401 3.7 14.7 0.6 CHB A:HEM401 3.7 13.2 0.4 CHB A:HEM401 3.7 18.9 0.6 CB A:CYS332 3.7 13.2 1.0 CHC A:HEM401 3.7 18.6 0.6 CHD A:HEM401 3.8 17.6 0.4 HA A:CYS332 3.9 17.5 1.0 O A:HOH698 3.9 36.9 1.0 C3D A:HEM401 4.2 13.8 0.6 C2D A:HEM401 4.2 14.1 0.6 H A:GLY334 4.3 17.6 1.0 C2A A:HEM401 4.3 14.6 0.6 C3A A:HEM401 4.3 12.9 0.6 C2B A:HEM401 4.3 18.9 0.6 C3C A:HEM401 4.3 9.0 0.6 C3B A:HEM401 4.3 19.3 0.6 C3D A:HEM401 4.3 15.6 0.4 C3B A:HEM401 4.3 17.2 0.4 C2B A:HEM401 4.3 16.1 0.4 C2A A:HEM401 4.3 11.6 0.4 C3A A:HEM401 4.3 8.2 0.4 C2D A:HEM401 4.3 15.7 0.4 C2C A:HEM401 4.3 10.3 0.6 C2C A:HEM401 4.3 15.0 0.4 C3C A:HEM401 4.3 10.8 0.4 CA A:CYS332 4.4 14.6 1.0 HB3 A:CYS332 4.5 15.9 1.0 HHA A:HEM401 4.6 15.8 0.6 HHA A:HEM401 4.6 18.6 0.4 HD1 A:PHE325 4.6 17.7 1.0 CD A:GLN228 4.6 29.9 1.0 HHC A:HEM401 4.6 20.6 0.4 HHD A:HEM401 4.6 17.6 0.6 HHB A:HEM401 4.6 15.8 0.4 HHB A:HEM401 4.6 22.7 0.6 HE22 A:GLN228 4.6 38.2 1.0 HD2 A:PHE271 4.6 19.9 1.0 HHC A:HEM401 4.7 22.4 0.6 HHD A:HEM401 4.7 21.2 0.4 HE2 A:PHE271 4.7 26.7 1.0 H A:LEU333 4.8 18.1 1.0 HB2 A:SER225 4.9 32.5 1.0 HA A:SER225 4.9 23.7 1.0

A.Greule, T.Izore, D.Machell, M.H.Hansen, M.Schoppet, J.J.De Voss, L.K.Charkoudian, R.B.Schittenhelm, J.R.Harmer, M.J.Cryle. The Cytochrome P450 Oxya From the Kistamicin Biosynthesis Cyclization Cascade Is Highly Sensitive to Oxidative Damage. Front Chem V. 10 68240 2022.
ISSN: ESSN 2296-2646
PubMed: 35464232
DOI: 10.3389/FCHEM.2022.868240