Iron in PDB 3wvs: Crystal Structure of Cytochrome P450REVI

The structure of Crystal Structure of Cytochrome P450REVI, PDB code: 3wvs was solved by S.Nagano, S.Takahashi, H.Osada, Y.Shiro, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.01 / 1.40
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	52.779, 73.472, 58.305, 90.00, 112.11, 90.00
R / Rfree (%)	17.3 / 18.8

The binding sites of Iron atom in the Crystal Structure of Cytochrome P450REVI (pdb code 3wvs). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Crystal Structure of Cytochrome P450REVI, PDB code: 3wvs:

Iron binding site 1 out of 1 in the Crystal Structure of Cytochrome P450REVI


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 P450REVI within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:5.6 occ:1.00 FE A:HEM501 0.0 5.6 1.0 NA A:HEM501 2.1 5.3 1.0 NC A:HEM501 2.1 5.7 1.0 NB A:HEM501 2.1 6.0 1.0 ND A:HEM501 2.1 5.9 1.0 SG A:CYS353 2.3 5.7 1.0 C4C A:HEM501 3.1 6.9 1.0 C4A A:HEM501 3.1 6.0 1.0 C1B A:HEM501 3.1 6.2 1.0 C1C A:HEM501 3.1 7.2 1.0 C1D A:HEM501 3.1 5.5 1.0 C4B A:HEM501 3.1 6.2 1.0 C4D A:HEM501 3.1 5.5 1.0 C1A A:HEM501 3.1 5.3 1.0 CB A:CYS353 3.4 5.8 1.0 CHB A:HEM501 3.4 6.8 1.0 CHD A:HEM501 3.4 6.5 1.0 CHC A:HEM501 3.4 6.2 1.0 CHA A:HEM501 3.5 5.4 1.0 CA A:CYS353 4.1 6.1 1.0 C3C A:HEM501 4.3 8.0 1.0 C2C A:HEM501 4.3 7.5 1.0 C3A A:HEM501 4.3 5.7 1.0 C2B A:HEM501 4.3 6.8 1.0 C3B A:HEM501 4.3 7.5 1.0 C2A A:HEM501 4.3 6.4 1.0 C2D A:HEM501 4.3 5.8 1.0 C3D A:HEM501 4.3 6.0 1.0 CAL A:RRM502 4.5 13.7 1.0 N A:GLY355 4.6 6.7 1.0 C A:CYS353 4.7 6.3 1.0 N A:LEU354 4.9 6.7 1.0 CAM A:RRM502 4.9 13.6 1.0 CA A:GLY355 4.9 6.8 1.0

S.Takahashi, S.Nagano, T.Nogawa, N.Kanoh, M.Uramoto, M.Kawatani, T.Shimizu, T.Miyazawa, Y.Shiro, H.Osada. Structure-Function Analyses of Cytochrome P450REVI Involved in Reveromycin A Biosynthesis and Evaluation of the Biological Activity of Its Substrate, Reveromycin T J.Biol.Chem. 2014.
ISSN: ESSN 1083-351X
PubMed: 25258320
DOI: 10.1074/JBC.M114.598391