Iron in PDB 2a1m: Crystal Structure of Ferrous Dioxygen Complex of Wild-Type Cytochrome P450CAM

All present enzymatic activity of Crystal Structure of Ferrous Dioxygen Complex of Wild-Type Cytochrome P450CAM:
1.14.15.1;

The structure of Crystal Structure of Ferrous Dioxygen Complex of Wild-Type Cytochrome P450CAM, PDB code: 2a1m was solved by S.Nagano, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.82 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	67.060, 62.290, 95.640, 90.00, 90.42, 90.00
R / Rfree (%)	19.1 / 24.7

The structure of Crystal Structure of Ferrous Dioxygen Complex of Wild-Type Cytochrome P450CAM also contains other interesting chemical elements:

Potassium

(K)

3 atoms

The binding sites of Iron atom in the Crystal Structure of Ferrous Dioxygen Complex of Wild-Type Cytochrome P450CAM (pdb code 2a1m). 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 Ferrous Dioxygen Complex of Wild-Type Cytochrome P450CAM, PDB code: 2a1m:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Ferrous Dioxygen Complex of Wild-Type Cytochrome P450CAM


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 Ferrous Dioxygen Complex of Wild-Type Cytochrome P450CAM within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe417 b:13.8 occ:1.00 FE A:HEM417 0.0 13.8 1.0 O1 A:OXY420 1.8 17.4 1.0 ND A:HEM417 2.0 12.4 1.0 NC A:HEM417 2.0 12.4 1.0 NB A:HEM417 2.0 11.6 1.0 NA A:HEM417 2.0 12.8 1.0 SG A:CYS357 2.3 12.0 1.0 O2 A:OXY420 2.8 21.8 1.0 C1D A:HEM417 3.0 14.4 1.0 C4C A:HEM417 3.1 14.3 1.0 C1C A:HEM417 3.1 12.8 1.0 C4D A:HEM417 3.1 12.1 1.0 C4B A:HEM417 3.1 11.2 1.0 C1B A:HEM417 3.1 10.5 1.0 C4A A:HEM417 3.1 11.9 1.0 C1A A:HEM417 3.1 11.2 1.0 CHD A:HEM417 3.4 14.5 1.0 CHC A:HEM417 3.4 9.8 1.0 CHB A:HEM417 3.4 8.3 1.0 CHA A:HEM417 3.5 13.6 1.0 CB A:CYS357 3.5 12.4 1.0 CA A:CYS357 4.2 11.1 1.0 C3D A:HEM417 4.3 13.2 1.0 C2D A:HEM417 4.3 12.8 1.0 C3B A:HEM417 4.3 8.9 1.0 C2C A:HEM417 4.3 13.3 1.0 C2B A:HEM417 4.3 9.1 1.0 C3C A:HEM417 4.3 15.4 1.0 C3A A:HEM417 4.3 12.5 1.0 C2A A:HEM417 4.3 11.0 1.0 C5 A:CAM1422 4.4 12.9 1.0 N A:GLY359 4.6 11.8 1.0 C9 A:CAM1422 4.8 12.5 1.0 C A:CYS357 4.8 14.2 1.0 N A:LEU358 4.8 12.5 1.0 OG1 A:THR252 4.9 13.6 1.0 C4 A:CAM1422 4.9 13.7 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Ferrous Dioxygen Complex of Wild-Type Cytochrome P450CAM


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 Ferrous Dioxygen Complex of Wild-Type Cytochrome P450CAM within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe417 b:16.0 occ:1.00 FE B:HEM417 0.0 16.0 1.0 O1 B:OXY420 1.8 16.2 1.0 NB B:HEM417 2.0 13.6 1.0 ND B:HEM417 2.0 13.8 1.0 NC B:HEM417 2.0 13.4 1.0 NA B:HEM417 2.0 15.5 1.0 SG B:CYS357 2.2 13.6 1.0 O2 B:OXY420 2.8 23.5 1.0 C4B B:HEM417 3.0 14.1 1.0 C1C B:HEM417 3.0 15.0 1.0 C1B B:HEM417 3.0 16.4 1.0 C4D B:HEM417 3.1 12.5 1.0 C1D B:HEM417 3.1 12.7 1.0 C1A B:HEM417 3.1 8.8 1.0 C4C B:HEM417 3.1 15.7 1.0 C4A B:HEM417 3.1 15.2 1.0 CB B:CYS357 3.4 13.4 1.0 CHC B:HEM417 3.4 12.2 1.0 CHA B:HEM417 3.4 13.6 1.0 CHB B:HEM417 3.4 13.8 1.0 CHD B:HEM417 3.5 13.8 1.0 CA B:CYS357 4.1 14.5 1.0 C2B B:HEM417 4.3 15.4 1.0 C2C B:HEM417 4.3 18.5 1.0 C3B B:HEM417 4.3 16.1 1.0 C2D B:HEM417 4.3 16.0 1.0 C3D B:HEM417 4.3 13.6 1.0 C3C B:HEM417 4.3 17.0 1.0 C2A B:HEM417 4.3 16.1 1.0 C3A B:HEM417 4.3 11.5 1.0 C5 B:CAM2422 4.6 18.2 1.0 N B:GLY359 4.7 19.3 1.0 C9 B:CAM2422 4.8 16.5 1.0 C B:CYS357 4.8 16.7 1.0 N B:LEU358 4.9 17.0 1.0 OG1 B:THR252 4.9 18.8 1.0

S.Nagano, T.L.Poulos. Crystallographic Study on the Dioxygen Complex of Wild-Type and Mutant Cytochrome P450CAM. Implications For the Dioxygen Activation Mechanism J.Biol.Chem. V. 280 31659 2005.
ISSN: ISSN 0021-9258
PubMed: 15994329
DOI: 10.1074/JBC.M505261200