Iron in PDB 4fmx: Crystal Structure of Substrate-Bound P450CIN

The structure of Crystal Structure of Substrate-Bound P450CIN, PDB code: 4fmx was solved by Y.Madrona, S.M.Tripathi, L.Huiying, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.99 / 1.55
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	57.551, 69.259, 122.608, 90.00, 97.14, 90.00
R / Rfree (%)	17.5 / 22

The binding sites of Iron atom in the Crystal Structure of Substrate-Bound P450CIN (pdb code 4fmx). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Substrate-Bound P450CIN, PDB code: 4fmx:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Substrate-Bound P450CIN


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 Substrate-Bound P450CIN within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:9.6 occ:1.00 FE A:HEM501 0.0 9.6 1.0 NB A:HEM501 2.1 7.6 1.0 NA A:HEM501 2.1 8.9 1.0 ND A:HEM501 2.1 9.3 1.0 NC A:HEM501 2.1 8.9 1.0 SG A:CYS347 2.4 10.7 1.0 C4B A:HEM501 3.1 7.8 1.0 C4D A:HEM501 3.1 10.9 1.0 C1C A:HEM501 3.1 8.5 1.0 C1B A:HEM501 3.1 8.4 1.0 C1A A:HEM501 3.1 9.0 1.0 C4A A:HEM501 3.1 9.4 1.0 C1D A:HEM501 3.1 9.3 1.0 C4C A:HEM501 3.2 9.4 1.0 HB2 A:CYS347 3.3 12.8 1.0 HA A:CYS347 3.4 11.1 1.0 CB A:CYS347 3.4 10.7 1.0 CHC A:HEM501 3.4 8.4 1.0 CHA A:HEM501 3.4 9.8 1.0 CHB A:HEM501 3.5 9.7 1.0 CHD A:HEM501 3.5 11.5 1.0 HD21 A:ASN242 3.8 16.7 1.0 H A:GLY349 3.8 14.0 1.0 CA A:CYS347 3.9 9.3 1.0 H A:LEU348 4.2 12.8 1.0 HB3 A:CYS347 4.2 12.8 1.0 C3B A:HEM501 4.3 9.4 1.0 C2B A:HEM501 4.3 8.6 1.0 C2C A:HEM501 4.3 8.9 1.0 C3A A:HEM501 4.3 10.2 1.0 C3D A:HEM501 4.3 10.5 1.0 C2A A:HEM501 4.3 9.9 1.0 C3C A:HEM501 4.3 10.3 1.0 C2D A:HEM501 4.3 10.8 1.0 HHC A:HEM501 4.4 10.1 1.0 ND2 A:ASN242 4.4 13.9 1.0 HHA A:HEM501 4.4 11.8 1.0 HHB A:HEM501 4.5 11.6 1.0 HHD A:HEM501 4.5 13.8 1.0 HD22 A:ASN242 4.5 16.7 1.0 N A:LEU348 4.6 10.7 1.0 C A:CYS347 4.6 10.5 1.0 N A:GLY349 4.7 11.7 1.0 HD22 A:LEU340 4.7 18.9 1.0 HA3 A:GLY349 4.8 14.7 1.0 C7 A:CNL502 4.8 18.2 1.0 HA3 A:GLY238 4.9 11.3 1.0 HA2 A:GLY238 4.9 11.3 1.0 HD23 A:LEU340 4.9 18.9 1.0 C2 A:CNL502 5.0 14.2 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Substrate-Bound P450CIN


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 Substrate-Bound P450CIN within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:15.7 occ:1.00 FE B:HEM501 0.0 15.7 1.0 NB B:HEM501 2.1 14.8 1.0 NA B:HEM501 2.1 14.8 1.0 ND B:HEM501 2.1 17.2 1.0 NC B:HEM501 2.1 16.2 1.0 SG B:CYS347 2.4 16.4 1.0 C4B B:HEM501 3.1 13.7 1.0 C1B B:HEM501 3.1 11.5 1.0 C4D B:HEM501 3.1 16.8 1.0 C1A B:HEM501 3.1 14.8 1.0 C1C B:HEM501 3.1 15.0 1.0 C4A B:HEM501 3.1 13.8 1.0 C1D B:HEM501 3.1 16.0 1.0 C4C B:HEM501 3.1 16.9 1.0 HB2 B:CYS347 3.2 19.2 1.0 CB B:CYS347 3.3 16.0 1.0 HA B:CYS347 3.4 20.0 1.0 CHC B:HEM501 3.4 14.4 1.0 CHA B:HEM501 3.4 15.9 1.0 CHB B:HEM501 3.5 12.4 1.0 CHD B:HEM501 3.5 15.5 1.0 H B:GLY349 3.8 19.9 1.0 HD21 B:ASN242 3.9 21.8 1.0 CA B:CYS347 3.9 16.7 1.0 H B:LEU348 4.2 21.0 1.0 HB3 B:CYS347 4.2 19.2 1.0 C2B B:HEM501 4.3 12.1 1.0 C3B B:HEM501 4.3 12.5 1.0 C2A B:HEM501 4.3 15.7 1.0 C3A B:HEM501 4.3 14.2 1.0 C2D B:HEM501 4.3 16.6 1.0 C3D B:HEM501 4.3 17.4 1.0 C2C B:HEM501 4.3 16.0 1.0 C3C B:HEM501 4.3 17.6 1.0 HHC B:HEM501 4.4 17.3 1.0 HHA B:HEM501 4.4 19.0 1.0 HHB B:HEM501 4.4 14.9 1.0 HHD B:HEM501 4.5 18.5 1.0 ND2 B:ASN242 4.5 18.2 1.0 N B:LEU348 4.5 17.6 1.0 C B:CYS347 4.6 16.0 1.0 HD22 B:ASN242 4.6 21.8 1.0 N B:GLY349 4.7 16.6 1.0 HD22 B:LEU340 4.7 21.1 1.0 HA3 B:GLY349 4.8 20.1 1.0 C2 B:CNL502 4.8 22.7 1.0 C7 B:CNL502 4.9 24.1 1.0 HA2 B:GLY238 5.0 18.6 1.0 HA3 B:GLY238 5.0 18.6 1.0

Y.Madrona, S.Tripathi, H.Li, T.L.Poulos. Crystal Structures of Substrate-Free and Nitrosyl Cytochrome P450CIN: Implications For O(2) Activation. Biochemistry V. 51 6623 2012.
ISSN: ISSN 0006-2960
PubMed: 22775403
DOI: 10.1021/BI300666U