Iron in PDB 1bk0: Isopenicillin N Synthase From Aspergillus Nidulans (Acv-Fe Complex)

The structure of Isopenicillin N Synthase From Aspergillus Nidulans (Acv-Fe Complex), PDB code: 1bk0 was solved by P.L.Roach, I.J.Clifton, C.M.H.Hensgens, N.Shibata, C.J.Schofield, J.Hajdu, J.E.Baldwin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	12.50 / 1.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	46.800, 71.500, 101.000, 90.00, 90.00, 90.00
R / Rfree (%)	17.2 / 19

The binding sites of Iron atom in the Isopenicillin N Synthase From Aspergillus Nidulans (Acv-Fe Complex) (pdb code 1bk0). 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 Isopenicillin N Synthase From Aspergillus Nidulans (Acv-Fe Complex), PDB code: 1bk0:

Iron binding site 1 out of 1 in the Isopenicillin N Synthase From Aspergillus Nidulans (Acv-Fe Complex)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Isopenicillin N Synthase From Aspergillus Nidulans (Acv-Fe Complex) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe350 b:6.5 occ:1.00 OD1 A:ASP216 2.1 6.3 1.0 O A:HOH713 2.1 11.4 1.0 NE2 A:HIS214 2.2 6.2 1.0 NE2 A:HIS270 2.2 7.0 1.0 S17 A:ACV351 2.4 6.4 1.0 CG A:ASP216 3.0 6.1 1.0 CE1 A:HIS270 3.1 6.7 1.0 CD2 A:HIS214 3.1 5.8 1.0 CE1 A:HIS214 3.2 6.0 1.0 CD2 A:HIS270 3.2 6.2 1.0 OD2 A:ASP216 3.3 6.7 1.0 C16 A:ACV351 3.4 6.5 1.0 C37 A:ACV351 3.9 14.3 1.0 ND1 A:HIS270 4.2 6.5 1.0 CG A:HIS214 4.3 6.4 1.0 O A:HOH712 4.3 11.5 1.0 ND1 A:HIS214 4.3 6.2 1.0 CG A:HIS270 4.3 6.3 1.0 CB A:ASP216 4.4 6.3 1.0 C33 A:ACV351 4.4 11.2 1.0 CA A:ASP216 4.7 6.8 1.0 C12 A:ACV351 4.8 6.8 1.0 N29 A:ACV351 4.8 8.7 1.0 C32 A:ACV351 4.8 11.5 1.0 O A:HOH710 4.8 8.3 1.0 N A:ASP216 4.9 7.0 1.0 C13 A:ACV351 4.9 6.8 1.0

P.L.Roach, I.J.Clifton, C.M.Hensgens, N.Shibata, C.J.Schofield, J.Hajdu, J.E.Baldwin. Structure of Isopenicillin N Synthase Complexed with Substrate and the Mechanism of Penicillin Formation. Nature V. 387 827 1997.
ISSN: ISSN 0028-0836
PubMed: 9194566
DOI: 10.1038/42990