Iron in PDB 9cjg: P450-G9 From Actinokineospora Terrae, A Non-Canonical, Serine-Ligated Cytochrome P450 in the Ligand-Free, Closed Conformation

The structure of P450-G9 From Actinokineospora Terrae, A Non-Canonical, Serine-Ligated Cytochrome P450 in the Ligand-Free, Closed Conformation, PDB code: 9cjg was solved by K.A.Ireland, K.M.Davis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	57.80 / 1.85
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	53.13, 59.65, 233.8, 90, 90, 90
R / Rfree (%)	21.4 / 24.3

The binding sites of Iron atom in the P450-G9 From Actinokineospora Terrae, A Non-Canonical, Serine-Ligated Cytochrome P450 in the Ligand-Free, Closed Conformation (pdb code 9cjg). 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-G9 From Actinokineospora Terrae, A Non-Canonical, Serine-Ligated Cytochrome P450 in the Ligand-Free, Closed Conformation, PDB code: 9cjg:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the P450-G9 From Actinokineospora Terrae, A Non-Canonical, Serine-Ligated Cytochrome P450 in the Ligand-Free, Closed Conformation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of P450-G9 From Actinokineospora Terrae, A Non-Canonical, Serine-Ligated Cytochrome P450 in the Ligand-Free, Closed Conformation within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:15.9 occ:1.00 FE A:HEM401 0.0 15.9 1.0 ND A:HEM401 1.9 7.6 1.0 NA A:HEM401 2.0 17.5 1.0 NC A:HEM401 2.1 14.8 1.0 NB A:HEM401 2.1 22.7 1.0 OG A:SER341 2.4 22.7 1.0 C4D A:HEM401 2.9 12.4 1.0 C1D A:HEM401 2.9 14.3 1.0 C1A A:HEM401 3.0 16.9 1.0 C4C A:HEM401 3.0 15.4 1.0 C4A A:HEM401 3.0 16.5 1.0 CB A:SER341 3.1 17.7 1.0 C1B A:HEM401 3.1 16.6 1.0 C4B A:HEM401 3.1 14.2 1.0 C1C A:HEM401 3.1 16.1 1.0 CHA A:HEM401 3.3 14.2 1.0 CHD A:HEM401 3.4 13.5 1.0 CHB A:HEM401 3.5 20.4 1.0 CHC A:HEM401 3.5 14.3 1.0 CB A:ALA230 3.7 20.7 1.0 CA A:SER341 3.9 20.4 1.0 C3D A:HEM401 4.1 11.4 1.0 C2D A:HEM401 4.1 11.2 1.0 C2A A:HEM401 4.2 17.2 1.0 C3A A:HEM401 4.2 21.7 1.0 C3C A:HEM401 4.2 17.4 1.0 C2C A:HEM401 4.3 17.2 1.0 C2B A:HEM401 4.3 19.9 1.0 C3B A:HEM401 4.3 22.2 1.0 CZ3 A:TRP229 4.4 20.4 1.0 N A:GLY343 4.6 21.2 1.0 N A:PHE342 4.6 15.6 1.0 CH2 A:TRP229 4.7 17.0 1.0 C A:SER341 4.7 15.6 1.0 ND2 A:ASN234 4.9 19.4 1.0 N A:SER341 5.0 13.5 1.0

Iron binding site 2 out of 2 in the P450-G9 From Actinokineospora Terrae, A Non-Canonical, Serine-Ligated Cytochrome P450 in the Ligand-Free, Closed Conformation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of P450-G9 From Actinokineospora Terrae, A Non-Canonical, Serine-Ligated Cytochrome P450 in the Ligand-Free, Closed Conformation within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe401 b:27.8 occ:1.00 FE B:HEM401 0.0 27.8 1.0 ND B:HEM401 1.9 21.2 1.0 NA B:HEM401 2.0 25.6 1.0 NC B:HEM401 2.1 24.8 1.0 NB B:HEM401 2.1 27.8 1.0 OG B:SER341 2.4 30.9 1.0 C4D B:HEM401 2.9 22.9 1.0 C1D B:HEM401 2.9 23.6 1.0 C1A B:HEM401 3.0 30.5 1.0 C4C B:HEM401 3.0 33.0 1.0 C4A B:HEM401 3.0 34.4 1.0 CB B:SER341 3.1 27.9 1.0 C1B B:HEM401 3.1 30.1 1.0 C4B B:HEM401 3.1 23.1 1.0 C1C B:HEM401 3.1 31.6 1.0 CHA B:HEM401 3.3 25.6 1.0 CHD B:HEM401 3.3 29.4 1.0 CHB B:HEM401 3.5 26.1 1.0 CHC B:HEM401 3.5 30.4 1.0 CB B:ALA230 3.7 26.8 1.0 CA B:SER341 3.9 29.0 1.0 C2D B:HEM401 4.1 22.6 1.0 C3D B:HEM401 4.1 25.2 1.0 C2A B:HEM401 4.2 27.8 1.0 C3A B:HEM401 4.2 29.7 1.0 C3C B:HEM401 4.2 25.8 1.0 C2C B:HEM401 4.2 31.1 1.0 C2B B:HEM401 4.3 27.7 1.0 C3B B:HEM401 4.3 33.8 1.0 CZ3 B:TRP229 4.5 28.4 1.0 N B:PHE342 4.6 32.5 1.0 C B:SER341 4.7 33.0 1.0 CH2 B:TRP229 4.8 31.6 1.0 N B:GLY343 4.8 35.4 1.0 ND2 B:ASN234 4.9 28.6 1.0

A.K.L.Nguy, K.A.Ireland, C.M.Kayrouz, J.C.Caceres, B.L.Greene, K.M.Davis, M.R.Seyedsayamdost. Non-Canonical Cytochrome P450 Enzymes in Nature. Biorxiv 2024.
ISSN: ISSN 2692-8205
PubMed: 39763895
DOI: 10.1101/2024.12.22.630014