Iron in PDB 1uob: Deacetoxycephalosporin C Synthase Complexed with 2-Oxoglutarate and Penicillin G

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

The structure of Deacetoxycephalosporin C Synthase Complexed with 2-Oxoglutarate and Penicillin G, PDB code: 1uob 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)	56.80 / 1.70
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	106.600, 106.600, 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 Penicillin G (pdb code 1uob). 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 Penicillin G, PDB code: 1uob:

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


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 Penicillin G within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1310 b:28.6 occ:1.00 NE2 A:HIS243 2.1 26.9 1.0 S1 A:PNN1311 2.1 80.7 0.5 O A:HOH2090 2.2 25.7 0.5 OD1 A:ASP185 2.2 26.5 1.0 O5 A:AKG1312 2.2 17.6 0.5 NE2 A:HIS183 2.3 31.3 1.0 O1 A:AKG1312 2.3 26.4 0.5 C2 A:PNN1311 2.6 79.8 0.5 C10 A:PNN1311 2.8 79.3 0.5 C9 A:PNN1311 2.8 78.9 0.5 C2 A:AKG1312 3.0 18.6 0.5 CE1 A:HIS243 3.1 28.9 1.0 C1 A:AKG1312 3.1 17.8 0.5 CD2 A:HIS243 3.1 33.1 1.0 CG A:ASP185 3.1 29.2 1.0 OD2 A:ASP185 3.2 31.0 1.0 CD2 A:HIS183 3.2 25.6 1.0 CE1 A:HIS183 3.2 42.3 1.0 C5 A:PNN1311 3.5 79.5 0.5 C3 A:PNN1311 4.1 80.8 0.5 CG2 A:ILE305 4.2 29.3 1.0 ND1 A:HIS243 4.2 30.4 1.0 CG A:HIS243 4.2 28.9 1.0 ND1 A:HIS183 4.3 35.0 1.0 O2 A:AKG1312 4.3 20.9 0.5 CG A:HIS183 4.3 29.4 1.0 N4 A:PNN1311 4.4 79.8 0.5 CB A:ASP185 4.5 24.5 1.0 C3 A:AKG1312 4.5 22.5 0.5 C6 A:PNN1311 4.9 79.0 0.5 CE2 A:PHE264 4.9 28.2 1.0 N A:ASP185 4.9 22.4 1.0 CD2 A:PHE225 4.9 33.9 1.0 CA A:ASP185 5.0 24.8 1.0 C4 A:AKG1312 5.0 23.3 0.5

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