Iron in PDB 1unb: Deacetoxycephalosporin C Synthase Complexed with 2-Oxoglutarate and Ampicillin

All present enzymatic activity of Deacetoxycephalosporin C Synthase Complexed with 2-Oxoglutarate and Ampicillin:
1.14.20.1;

The structure of Deacetoxycephalosporin C Synthase Complexed with 2-Oxoglutarate and Ampicillin, PDB code: 1unb 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)	31.50 / 1.50
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	106.700, 106.700, 71.600, 90.00, 90.00, 120.00
R / Rfree (%)	18.9 / 23.6

The binding sites of Iron atom in the Deacetoxycephalosporin C Synthase Complexed with 2-Oxoglutarate and Ampicillin (pdb code 1unb). 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 2-Oxoglutarate and Ampicillin, PDB code: 1unb:

Iron binding site 1 out of 1 in the Deacetoxycephalosporin C Synthase Complexed with 2-Oxoglutarate and Ampicillin


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 2-Oxoglutarate and Ampicillin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1310 b:16.4 occ:1.00 NE2 A:HIS243 2.1 17.7 1.0 OD1 A:ASP185 2.1 14.1 1.0 S1 A:PN11312 2.1 39.1 0.5 O5 A:AKG1311 2.2 8.4 0.5 NE2 A:HIS183 2.2 19.0 1.0 O1 A:AKG1311 2.3 20.0 0.5 O A:HOH2114 2.3 15.9 0.5 C1 A:PN11312 2.5 39.2 0.5 C6 A:PN11312 2.6 40.2 0.5 C2 A:AKG1311 2.9 8.9 0.5 C16 A:PN11312 2.9 40.3 0.5 C1 A:AKG1311 2.9 10.8 0.5 CE1 A:HIS243 3.0 15.3 1.0 CG A:ASP185 3.1 17.4 1.0 CD2 A:HIS243 3.1 19.6 1.0 CD2 A:HIS183 3.2 15.1 1.0 CE1 A:HIS183 3.2 23.9 1.0 OD2 A:ASP185 3.2 17.8 1.0 C13 A:PN11312 3.4 41.0 0.5 C12 A:PN11312 4.0 41.7 0.5 ND1 A:HIS243 4.1 20.0 1.0 CG A:HIS243 4.2 16.3 1.0 CG2 A:ILE305 4.2 16.7 1.0 O2 A:AKG1311 4.2 14.9 0.5 ND1 A:HIS183 4.3 21.7 1.0 CG A:HIS183 4.3 16.3 1.0 N3 A:PN11312 4.3 41.3 0.5 C3 A:AKG1311 4.4 13.0 0.5 CB A:ASP185 4.5 14.5 1.0 C14 A:PN11312 4.8 42.0 0.5 C2 A:PN11312 4.9 41.8 0.5 CA A:ASP185 4.9 13.8 1.0 N A:ASP185 4.9 15.2 1.0 CE2 A:PHE264 4.9 20.3 1.0 C4 A:AKG1311 5.0 14.5 0.5 CD2 A:PHE225 5.0 20.9 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