Iron in PDB 1rxf: Deacetoxycephalosporin C Synthase Complexed with Fe(II)

The structure of Deacetoxycephalosporin C Synthase Complexed with Fe(II), PDB code: 1rxf was solved by K.Valegard, A.C.Terwisscha Van Scheltinga, M.D.Lloyd, T.Hara, S.Ramaswamy, A.Perrakis, A.Thompson, H.J.Lee, J.E.Baldwin, C.J.Schofield, J.Hajdu, I.Andersson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.50
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	106.100, 106.100, 71.200, 90.00, 90.00, 120.00
R / Rfree (%)	11.9 / 14.2

The binding sites of Iron atom in the Deacetoxycephalosporin C Synthase Complexed with Fe(II) (pdb code 1rxf). 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 Deacetoxycephalosporin C Synthase Complexed with Fe(II), PDB code: 1rxf:

Iron binding site 1 out of 1 in the Deacetoxycephalosporin C Synthase Complexed with Fe(II)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Deacetoxycephalosporin C Synthase Complexed with Fe(II) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe312 b:19.3 occ:1.00 O A:HOH630 2.1 23.2 1.0 O A:HOH628 2.1 24.2 1.0 OD1 A:ASP185 2.1 18.4 1.0 NE2 A:HIS243 2.2 19.1 1.0 NE2 A:HIS183 2.2 20.5 1.0 O A:HOH629 2.2 24.9 1.0 CD2 A:HIS183 3.1 19.8 1.0 CG A:ASP185 3.1 19.8 1.0 CD2 A:HIS243 3.1 20.4 1.0 CE1 A:HIS243 3.2 19.3 1.0 CE1 A:HIS183 3.2 22.9 1.0 OD2 A:ASP185 3.3 19.8 1.0 CG2 A:ILE305 4.1 23.4 1.0 ND1 A:HIS243 4.3 20.7 1.0 CG A:HIS183 4.3 20.9 1.0 ND1 A:HIS183 4.3 23.5 1.0 CG A:HIS243 4.3 21.1 1.0 O A:HOH647 4.3 36.4 1.0 CB A:ASP185 4.5 17.4 1.0 CD2 A:PHE225 4.9 22.6 1.0 N A:ASP185 4.9 16.8 1.0 CA A:ASP185 4.9 16.6 1.0 CE2 A:PHE225 5.0 22.5 1.0

K.Valegard, A.C.Van Scheltinga, M.D.Lloyd, T.Hara, S.Ramaswamy, A.Perrakis, A.Thompson, H.J.Lee, J.E.Baldwin, C.J.Schofield, J.Hajdu, I.Andersson. Structure of A Cephalosporin Synthase. Nature V. 394 805 1998.
ISSN: ISSN 0028-0836
PubMed: 9723623
DOI: 10.1038/29575