Iron in PDB 1blz: Isopenicillin N Synthase From Aspergillus Nidulans (Acv-Fe- No Complex)

The structure of Isopenicillin N Synthase From Aspergillus Nidulans (Acv-Fe- No Complex), PDB code: 1blz 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)	30.00 / 1.45
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	47.260, 73.080, 101.940, 90.00, 90.00, 90.00
R / Rfree (%)	20.5 / 21.7

The binding sites of Iron atom in the Isopenicillin N Synthase From Aspergillus Nidulans (Acv-Fe- No Complex) (pdb code 1blz). 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- No Complex), PDB code: 1blz:

Iron binding site 1 out of 1 in the Isopenicillin N Synthase From Aspergillus Nidulans (Acv-Fe- No 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- No Complex) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe332 b:16.7 occ:1.00 N A:NO334 2.1 26.1 1.0 OD1 A:ASP216 2.2 16.1 1.0 NE2 A:HIS270 2.2 15.6 1.0 NE2 A:HIS214 2.3 16.6 1.0 O A:HOH650 2.3 21.1 1.0 S17 A:ACV333 2.4 17.6 1.0 O A:NO334 2.9 24.4 1.0 CE1 A:HIS270 3.2 16.0 1.0 CG A:ASP216 3.2 16.2 1.0 CD2 A:HIS270 3.2 15.0 1.0 CE1 A:HIS214 3.2 16.5 1.0 CD2 A:HIS214 3.3 16.6 1.0 C16 A:ACV333 3.5 16.7 1.0 OD2 A:ASP216 3.5 18.0 1.0 ND1 A:HIS270 4.3 16.1 1.0 CG A:HIS270 4.3 15.2 1.0 ND1 A:HIS214 4.3 16.6 1.0 CG A:HIS214 4.4 15.4 1.0 C33 A:ACV333 4.4 18.3 1.0 O A:HOH560 4.4 25.3 1.0 CB A:ASP216 4.5 16.4 1.0 N29 A:ACV333 4.7 17.2 1.0 C12 A:ACV333 4.8 17.2 1.0 C37 A:ACV333 4.8 19.1 1.0 CA A:ASP216 4.8 15.5 1.0 O A:HOH514 4.9 18.8 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