Iron in PDB 1uog: Deacetoxycephalosporin C Synthase Complexed with Deacetoxycephalosporin C

All present enzymatic activity of Deacetoxycephalosporin C Synthase Complexed with Deacetoxycephalosporin C:
1.14.20.1;

The structure of Deacetoxycephalosporin C Synthase Complexed with Deacetoxycephalosporin C, PDB code: 1uog was solved by K.Valegard, A.C.Terwisscha Van Scheltinga, A.Dubus, L.M.Oster, G.Rhangino, J.Hajdu, I.Andersson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.40 / 1.70
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	106.600, 106.600, 74.000, 90.00, 90.00, 120.00
R / Rfree (%)	20.4 / 24.2

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

Iron binding site 1 out of 1 in the Deacetoxycephalosporin C Synthase Complexed with Deacetoxycephalosporin C


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 Deacetoxycephalosporin C within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1312 b:82.5 occ:1.00 NE2 A:HIS243 1.9 36.3 1.0 NE2 A:HIS183 2.1 36.5 1.0 OD1 A:ASP185 2.1 29.6 1.0 C37 A:P1C1311 2.5 44.1 1.0 CD2 A:HIS183 2.6 26.2 1.0 CD2 A:HIS243 2.6 38.9 1.0 S A:P1C1311 2.8 67.0 1.0 CE1 A:HIS243 3.0 36.5 1.0 CG A:ASP185 3.0 30.4 1.0 C16 A:P1C1311 3.1 69.3 1.0 OD2 A:ASP185 3.1 26.0 1.0 CE1 A:HIS183 3.3 33.7 1.0 C32 A:P1C1311 3.3 57.3 1.0 N29 A:P1C1311 3.5 72.8 1.0 C30 A:P1C1311 3.7 66.4 1.0 CG A:HIS243 3.8 37.0 1.0 CG A:HIS183 3.8 25.5 1.0 ND1 A:HIS243 4.0 33.6 1.0 ND1 A:HIS183 4.1 33.0 1.0 CG2 A:ILE305 4.2 25.3 1.0 C33 A:P1C1311 4.4 59.0 1.0 CB A:ASP185 4.4 22.3 1.0 O A:HIS183 4.6 26.1 1.0 CD2 A:PHE225 4.6 40.9 1.0 N A:ASP185 4.6 20.9 1.0 C12 A:P1C1311 4.6 64.0 1.0 C13 A:P1C1311 4.8 71.3 1.0 C A:TYR184 4.8 21.7 1.0 CA A:ASP185 4.8 21.3 1.0 CE2 A:PHE225 4.8 35.6 1.0 C31 A:P1C1311 4.8 70.0 1.0 O A:TYR184 5.0 18.9 1.0

K.Valegard, A.C.Terwisscha Van Scheltinga, A.Dubus, G.Ranghino, L.M.Oster, J.Hajdu, I.Andersson. The Structural Basis of Cephalosporin Formation in A Mononuclear Ferrous Enzyme Nat.Struct.Mol.Biol. V. 11 95 2004.
ISSN: ISSN 1545-9993
PubMed: 14718929
DOI: 10.1038/NSMB712