Iron in PDB 2ca3: Sulfite Dehydrogenase From Starkeya Novella R55M Mutant

The structure of Sulfite Dehydrogenase From Starkeya Novella R55M Mutant, PDB code: 2ca3 was solved by S.Bailey, U.Kappler, C.Feng, M.J.Honeychurch, P.V.Bernhardt, G.Tollin, J.H.Enemark, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.00
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	97.654, 93.321, 56.035, 90.00, 90.00, 90.00
R / Rfree (%)	16.1 / 20.6

The structure of Sulfite Dehydrogenase From Starkeya Novella R55M Mutant also contains other interesting chemical elements:

Molybdenum

(Mo)

1 atom

The binding sites of Iron atom in the Sulfite Dehydrogenase From Starkeya Novella R55M Mutant (pdb code 2ca3). 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 Sulfite Dehydrogenase From Starkeya Novella R55M Mutant, PDB code: 2ca3:

Iron binding site 1 out of 1 in the Sulfite Dehydrogenase From Starkeya Novella R55M Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Sulfite Dehydrogenase From Starkeya Novella R55M Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe1582 b:17.4 occ:1.00 FE B:HEC1582 0.0 17.4 1.0 NE2 B:HIS533 2.0 13.1 1.0 NC B:HEC1582 2.0 18.1 1.0 NB B:HEC1582 2.1 19.2 1.0 NA B:HEC1582 2.1 18.9 1.0 ND B:HEC1582 2.1 20.2 1.0 SD B:MET557 2.3 17.0 1.0 CE1 B:HIS533 2.9 14.5 1.0 CD2 B:HIS533 3.0 14.3 1.0 C4C B:HEC1582 3.0 20.7 1.0 C1C B:HEC1582 3.0 19.2 1.0 C4B B:HEC1582 3.0 17.1 1.0 C1B B:HEC1582 3.1 18.2 1.0 C4A B:HEC1582 3.1 17.8 1.0 C1D B:HEC1582 3.1 20.4 1.0 C4D B:HEC1582 3.1 16.3 1.0 C1A B:HEC1582 3.1 15.4 1.0 CHC B:HEC1582 3.4 16.8 1.0 CE B:MET557 3.4 12.6 1.0 CHD B:HEC1582 3.4 20.0 1.0 CHB B:HEC1582 3.5 19.0 1.0 CHA B:HEC1582 3.5 16.0 1.0 CG B:MET557 3.5 17.1 1.0 ND1 B:HIS533 4.0 13.3 1.0 CG B:HIS533 4.1 14.4 1.0 C3C B:HEC1582 4.2 19.9 1.0 C3B B:HEC1582 4.3 18.0 1.0 C2C B:HEC1582 4.3 18.2 1.0 C2B B:HEC1582 4.3 20.5 1.0 C3A B:HEC1582 4.3 13.0 1.0 C2A B:HEC1582 4.3 12.5 1.0 C3D B:HEC1582 4.3 17.3 1.0 C2D B:HEC1582 4.3 20.3 1.0 CB B:MET557 4.4 23.3 1.0 O B:HOH2039 4.6 15.2 1.0

S.Bailey, T.Rapson, K.Johnson-Winters, A.V.Astashkin, J.H.Enemark, U.Kappler. Molecular Basis For Enzymatic Sulfite Oxidation: How Three Conserved Active Site Residues Shape Enzyme Activity. J.Biol.Chem. V. 284 2053 2009.
ISSN: ISSN 0021-9258
PubMed: 19004819
DOI: 10.1074/JBC.M807718200