Iron in PDB 1r0q: Characterization of the Conversion of the Malformed, Recombinant Cytochrome RC552 to A 2-Formyl-4-Vinyl (Spirographis) Heme

The structure of Characterization of the Conversion of the Malformed, Recombinant Cytochrome RC552 to A 2-Formyl-4-Vinyl (Spirographis) Heme, PDB code: 1r0q was solved by J.A.Fee, T.R.Todaro, E.Luna, D.Sanders, L.M.Hunsicker-Wang, K.M.Patel, K.L.Bren, E.Gomez-Moran, M.G.Hill, J.Ai, T.M.Loehr, W.A.Oertling, P.A.Williams, C.D.Stout, D.Mcree, A.Pastuszyn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.61
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	86.770, 86.770, 31.840, 90.00, 90.00, 120.00
R / Rfree (%)	18.6 / 25.5

The binding sites of Iron atom in the Characterization of the Conversion of the Malformed, Recombinant Cytochrome RC552 to A 2-Formyl-4-Vinyl (Spirographis) Heme (pdb code 1r0q). 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 Characterization of the Conversion of the Malformed, Recombinant Cytochrome RC552 to A 2-Formyl-4-Vinyl (Spirographis) Heme, PDB code: 1r0q:

Iron binding site 1 out of 1 in the Characterization of the Conversion of the Malformed, Recombinant Cytochrome RC552 to A 2-Formyl-4-Vinyl (Spirographis) Heme


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Characterization of the Conversion of the Malformed, Recombinant Cytochrome RC552 to A 2-Formyl-4-Vinyl (Spirographis) Heme within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe200 b:8.3 occ:1.00 FE A:HFM200 0.0 8.3 1.0 NC A:HFM200 2.0 8.4 1.0 NB A:HFM200 2.0 4.9 1.0 NE2 A:HIS15 2.0 8.9 1.0 ND A:HFM200 2.1 7.6 1.0 NA A:HFM200 2.1 6.6 1.0 SD A:MET69 2.3 7.9 1.0 CE1 A:HIS15 3.0 8.3 1.0 C1C A:HFM200 3.0 11.0 1.0 C1B A:HFM200 3.0 9.3 1.0 C4A A:HFM200 3.0 9.4 1.0 C4B A:HFM200 3.0 9.2 1.0 C4D A:HFM200 3.0 7.2 1.0 C4C A:HFM200 3.1 10.4 1.0 C1D A:HFM200 3.1 10.3 1.0 C1A A:HFM200 3.1 9.2 1.0 CD2 A:HIS15 3.1 7.6 1.0 CE A:MET69 3.3 12.3 1.0 CHC A:HFM200 3.4 10.8 1.0 CHD A:HFM200 3.4 6.4 1.0 CHB A:HFM200 3.4 11.7 1.0 CHA A:HFM200 3.4 10.6 1.0 CG A:MET69 3.4 10.0 1.0 CB A:MET69 4.1 9.0 1.0 ND1 A:HIS15 4.1 6.8 1.0 CG A:HIS15 4.2 9.1 1.0 C3B A:HFM200 4.2 7.0 1.0 C2B A:HFM200 4.2 7.6 1.0 C2D A:HFM200 4.3 9.2 1.0 C3C A:HFM200 4.3 11.3 1.0 C2C A:HFM200 4.3 8.9 1.0 C2A A:HFM200 4.3 9.4 1.0 C3D A:HFM200 4.3 8.8 1.0 C3A A:HFM200 4.3 6.0 1.0

J.A.Fee, T.R.Todaro, E.Luna, D.Sanders, L.M.Hunsicker-Wang, K.M.Patel, K.L.Bren, E.Gomez-Moran, M.G.Hill, J.Ai, T.M.Loehr, W.A.Oertling, P.A.Williams, C.D.Stout, D.Mcree, A.Pastuszyn. Cytochrome RC552, Formed During Expression of the Truncated, Thermus Thermophilus Cytochrome C552 Gene in the Cytoplasm of Escherichia Coli, Reacts Spontaneously to Form Protein-Bound 2-Formyl-4-Vinyl (Spirographis) Heme. Biochemistry V. 43 12162 2004.
ISSN: ISSN 0006-2960
PubMed: 15379555
DOI: 10.1021/BI048968L