Iron in PDB 2rfb: Crystal Structure of A Cytochrome P450 From the Thermoacidophilic Archaeon Picrophilus Torridus

All present enzymatic activity of Crystal Structure of A Cytochrome P450 From the Thermoacidophilic Archaeon Picrophilus Torridus:
1.14.14.1;

The structure of Crystal Structure of A Cytochrome P450 From the Thermoacidophilic Archaeon Picrophilus Torridus, PDB code: 2rfb was solved by W.W.Ho, H.Li, T.L.Poulos, C.R.Nishida, P.R.Ortiz De Montellano, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.51 / 2.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	48.790, 168.460, 88.230, 90.00, 96.25, 90.00
R / Rfree (%)	21.1 / 26.8

The binding sites of Iron atom in the Crystal Structure of A Cytochrome P450 From the Thermoacidophilic Archaeon Picrophilus Torridus (pdb code 2rfb). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the Crystal Structure of A Cytochrome P450 From the Thermoacidophilic Archaeon Picrophilus Torridus, PDB code: 2rfb:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the Crystal Structure of A Cytochrome P450 From the Thermoacidophilic Archaeon Picrophilus Torridus


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 A Cytochrome P450 From the Thermoacidophilic Archaeon Picrophilus Torridus within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe410 b:66.1 occ:1.00 FE A:HEM410 0.0 66.1 1.0 ND A:HEM410 2.0 67.1 1.0 NB A:HEM410 2.1 68.8 1.0 NA A:HEM410 2.1 66.6 1.0 NC A:HEM410 2.1 68.0 1.0 SG A:CYS304 2.3 65.2 1.0 C4D A:HEM410 3.0 68.2 1.0 C4B A:HEM410 3.0 69.0 1.0 C1D A:HEM410 3.0 65.9 1.0 C1A A:HEM410 3.1 67.7 1.0 C4C A:HEM410 3.1 65.0 1.0 C1C A:HEM410 3.1 68.5 1.0 C4A A:HEM410 3.2 66.9 1.0 C1B A:HEM410 3.3 69.7 1.0 CB A:CYS304 3.4 65.9 1.0 CHC A:HEM410 3.4 68.3 1.0 CHA A:HEM410 3.4 67.1 1.0 CHD A:HEM410 3.5 67.0 1.0 CHB A:HEM410 3.7 69.4 1.0 O A:GLY197 3.9 74.8 1.0 CA A:CYS304 4.0 65.8 1.0 C3D A:HEM410 4.2 67.5 1.0 C2D A:HEM410 4.2 66.1 1.0 C3B A:HEM410 4.3 71.3 1.0 C3C A:HEM410 4.3 67.6 1.0 C2A A:HEM410 4.4 69.3 1.0 C2C A:HEM410 4.4 69.2 1.0 C3A A:HEM410 4.4 68.0 1.0 C2B A:HEM410 4.4 70.3 1.0 N A:GLY306 4.6 68.4 1.0 C A:CYS304 4.7 66.0 1.0 C A:GLY197 4.7 73.7 1.0 N A:LEU305 4.7 65.7 1.0

Iron binding site 2 out of 3 in the Crystal Structure of A Cytochrome P450 From the Thermoacidophilic Archaeon Picrophilus Torridus


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 A Cytochrome P450 From the Thermoacidophilic Archaeon Picrophilus Torridus within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe410 b:65.2 occ:1.00 FE B:HEM410 0.0 65.2 1.0 NA B:HEM410 2.1 65.8 1.0 ND B:HEM410 2.1 65.9 1.0 NB B:HEM410 2.1 62.4 1.0 NC B:HEM410 2.1 65.3 1.0 SG B:CYS304 2.1 66.9 1.0 C1A B:HEM410 3.0 65.2 1.0 C4D B:HEM410 3.1 65.8 1.0 C4B B:HEM410 3.1 61.6 1.0 C4C B:HEM410 3.1 65.1 1.0 C1D B:HEM410 3.1 65.3 1.0 C1B B:HEM410 3.1 62.4 1.0 C4A B:HEM410 3.1 64.7 1.0 C1C B:HEM410 3.1 65.0 1.0 CB B:CYS304 3.3 68.5 1.0 CHA B:HEM410 3.4 64.3 1.0 CHD B:HEM410 3.4 65.1 1.0 CHC B:HEM410 3.4 62.8 1.0 CHB B:HEM410 3.5 62.6 1.0 CA B:CYS304 4.0 68.0 1.0 O B:GLY197 4.1 73.2 1.0 C3B B:HEM410 4.3 63.0 1.0 C2A B:HEM410 4.3 65.1 1.0 C2B B:HEM410 4.3 64.0 1.0 C3C B:HEM410 4.3 65.6 1.0 C3D B:HEM410 4.3 67.0 1.0 C3A B:HEM410 4.3 65.1 1.0 C2D B:HEM410 4.3 66.9 1.0 C2C B:HEM410 4.3 66.9 1.0 N B:GLY306 4.6 71.6 1.0 C B:GLY197 4.6 72.6 1.0 C B:CYS304 4.7 69.0 1.0 N B:LEU305 4.7 69.8 1.0 CA B:GLY197 4.9 71.8 1.0 CA B:GLY306 5.0 71.2 1.0

Iron binding site 3 out of 3 in the Crystal Structure of A Cytochrome P450 From the Thermoacidophilic Archaeon Picrophilus Torridus


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of A Cytochrome P450 From the Thermoacidophilic Archaeon Picrophilus Torridus within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe410 b:64.9 occ:1.00 FE C:HEM410 0.0 64.9 1.0 ND C:HEM410 2.0 64.3 1.0 NC C:HEM410 2.0 64.5 1.0 NA C:HEM410 2.0 64.5 1.0 NB C:HEM410 2.1 63.5 1.0 SG C:CYS304 2.3 64.1 1.0 C4D C:HEM410 3.0 64.5 1.0 C1A C:HEM410 3.0 65.3 1.0 C1C C:HEM410 3.0 64.5 1.0 C4B C:HEM410 3.0 63.1 1.0 C1D C:HEM410 3.0 63.4 1.0 C4C C:HEM410 3.0 64.6 1.0 C4A C:HEM410 3.1 64.8 1.0 C1B C:HEM410 3.1 63.9 1.0 CHA C:HEM410 3.3 64.2 1.0 CHC C:HEM410 3.4 63.6 1.0 CHD C:HEM410 3.4 64.3 1.0 CB C:CYS304 3.4 65.3 1.0 CHB C:HEM410 3.5 64.7 1.0 CA C:CYS304 4.0 64.8 1.0 C3D C:HEM410 4.2 64.3 1.0 C3C C:HEM410 4.2 63.4 1.0 C2C C:HEM410 4.2 63.9 1.0 C2D C:HEM410 4.2 63.3 1.0 C3B C:HEM410 4.3 64.9 1.0 C2A C:HEM410 4.3 66.6 1.0 C3A C:HEM410 4.3 66.3 1.0 C2B C:HEM410 4.3 63.8 1.0 O C:GLY197 4.4 72.0 1.0 C C:GLY197 4.6 72.0 1.0 N C:GLY306 4.7 65.9 1.0 N C:LEU305 4.7 65.0 1.0 CA C:GLY197 4.7 71.8 1.0 C C:CYS304 4.7 65.0 1.0

W.W.Ho, H.Li, C.R.Nishida, P.R.Ortiz De Montellano, T.L.Poulos. Crystal Structure and Properties of CYP231A2 From the Thermoacidophilic Archaeon Picrophilus Torridus. Biochemistry V. 47 2071 2008.
ISSN: ISSN 0006-2960
PubMed: 18197710
DOI: 10.1021/BI702240K