Iron in PDB 3vym: Dimeric Hydrogenobacter Thermophilus Cytochrome C552

The structure of Dimeric Hydrogenobacter Thermophilus Cytochrome C552, PDB code: 3vym was solved by Y.Hayashi, S.Nagao, H.Osuka, H.Komori, Y.Higuchi, S.Hirota, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.97 / 2.00
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	46.148, 46.148, 78.407, 90.00, 90.00, 120.00
R / Rfree (%)	20.4 / 26.4

The binding sites of Iron atom in the Dimeric Hydrogenobacter Thermophilus Cytochrome C552 (pdb code 3vym). 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 Dimeric Hydrogenobacter Thermophilus Cytochrome C552, PDB code: 3vym:

Iron binding site 1 out of 1 in the Dimeric Hydrogenobacter Thermophilus Cytochrome C552


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Dimeric Hydrogenobacter Thermophilus Cytochrome C552 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe101 b:27.2 occ:1.00 FE A:HEC101 0.0 27.2 1.0 NE2 A:HIS14 1.9 22.9 1.0 NB A:HEC101 2.0 22.8 1.0 NC A:HEC101 2.0 30.6 1.0 ND A:HEC101 2.1 27.9 1.0 NA A:HEC101 2.1 25.8 1.0 CE1 A:HIS14 2.7 25.1 1.0 C4B A:HEC101 3.0 26.2 1.0 C1C A:HEC101 3.0 29.8 1.0 C1B A:HEC101 3.0 24.9 1.0 CD2 A:HIS14 3.0 29.9 1.0 C4C A:HEC101 3.0 31.9 1.0 C4A A:HEC101 3.1 27.5 1.0 C4D A:HEC101 3.1 29.6 1.0 C1D A:HEC101 3.1 30.8 1.0 C1A A:HEC101 3.1 30.2 1.0 CHC A:HEC101 3.3 28.3 1.0 CHB A:HEC101 3.4 19.7 1.0 CHD A:HEC101 3.5 30.1 1.0 CHA A:HEC101 3.5 26.5 1.0 ND1 A:HIS14 3.9 23.7 1.0 CG A:HIS14 4.1 27.5 1.0 C3C A:HEC101 4.2 30.2 1.0 C2C A:HEC101 4.2 28.1 1.0 C3B A:HEC101 4.3 23.7 1.0 C2B A:HEC101 4.3 23.1 1.0 C3D A:HEC101 4.3 29.9 1.0 C2A A:HEC101 4.3 28.3 1.0 C2D A:HEC101 4.3 30.3 1.0 C3A A:HEC101 4.3 28.2 1.0

Y.Hayashi, S.Nagao, H.Osuka, H.Komori, Y.Higuchi, S.Hirota. Domain Swapping of the Heme and N-Terminal Alpha-Helix in Hydrogenobacter Thermophilus Cytochrome C(552) Dimer Biochemistry V. 51 8608 2012.
ISSN: ISSN 0006-2960
PubMed: 23035813
DOI: 10.1021/BI3011303