Iron in PDB 1qiq: Isopenicillin N Synthase From Aspergillus Nidulans (Acmc Fe Complex)

The structure of Isopenicillin N Synthase From Aspergillus Nidulans (Acmc Fe Complex), PDB code: 1qiq was solved by P.J.Rutledge, I.J.Clifton, N.I.Burzlaff, P.L.Roach, R.M.Adlington, J.E.Baldwin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 1.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	46.810, 71.660, 101.630, 90.00, 90.00, 90.00
R / Rfree (%)	17.3 / 19.9

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

Iron binding site 1 out of 1 in the Isopenicillin N Synthase From Aspergillus Nidulans (Acmc 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 (Acmc Fe Complex) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe333 b:8.0 occ:1.00 OD1 A:ASP216 2.2 8.3 1.0 O A:HOH2289 2.2 9.8 1.0 NE2 A:HIS214 2.2 8.7 1.0 NE2 A:HIS270 2.3 8.8 1.0 S37 A:ACC332 2.4 8.0 1.0 S41 A:ACC332 2.7 9.2 1.0 CE1 A:HIS270 3.2 9.6 1.0 CD2 A:HIS214 3.2 8.7 1.0 CG A:ASP216 3.2 7.7 1.0 CE1 A:HIS214 3.2 7.3 1.0 CD2 A:HIS270 3.3 9.1 1.0 OD2 A:ASP216 3.4 7.9 1.0 C35 A:ACC332 3.5 8.4 1.0 C5 A:ACC332 3.7 12.0 1.0 C42 A:ACC332 3.8 11.4 1.0 O A:HOH2331 4.2 12.7 1.0 ND1 A:HIS270 4.3 9.3 1.0 CG A:HIS214 4.3 8.2 1.0 ND1 A:HIS214 4.3 7.5 1.0 CG A:HIS270 4.4 8.8 1.0 CB A:ASP216 4.5 8.3 1.0 N2 A:ACC332 4.7 10.8 1.0 C3 A:ACC332 4.8 10.3 1.0 CA A:ASP216 4.8 8.2 1.0 C4 A:ACC332 4.8 10.7 1.0 C1 A:ACC332 4.9 10.9 1.0 O A:HOH2290 4.9 8.2 1.0

N.I.Burzlaff, P.J.Rutledge, I.J.Clifton, C.M.H.Hensgens, M.Pickford, R.M.Adlington, P.L.Roach, J.E.Baldwin. The Reaction Cycle of Isopenicillin N Synthase Observed By X-Ray Diffraction. Nature V. 401 721 1999.
ISSN: ISSN 0028-0836
PubMed: 10537113
DOI: 10.1038/44400