Iron in PDB 1w03: Isopenicillin N Synthase Aminoadipoyl-Cysteinyl-Glycine-Fe Complex

All present enzymatic activity of Isopenicillin N Synthase Aminoadipoyl-Cysteinyl-Glycine-Fe Complex:
1.21.3.1;

The structure of Isopenicillin N Synthase Aminoadipoyl-Cysteinyl-Glycine-Fe Complex, PDB code: 1w03 was solved by A.J.Long, I.J.Clifton, P.J.Rutledge, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	11.99 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	46.770, 71.200, 100.970, 90.00, 90.00, 90.00
R / Rfree (%)	17.1 / 19.7

The binding sites of Iron atom in the Isopenicillin N Synthase Aminoadipoyl-Cysteinyl-Glycine-Fe Complex (pdb code 1w03). 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 Aminoadipoyl-Cysteinyl-Glycine-Fe Complex, PDB code: 1w03:

Iron binding site 1 out of 1 in the Isopenicillin N Synthase Aminoadipoyl-Cysteinyl-Glycine-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 Aminoadipoyl-Cysteinyl-Glycine-Fe Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1333 b:29.6 occ:1.00 OD1 A:ASP216 2.2 18.2 1.0 NE2 A:HIS214 2.3 14.3 1.0 O A:HOH2266 2.3 27.5 1.0 O A:HOH2188 2.3 26.1 1.0 NE2 A:HIS270 2.3 16.1 1.0 S17 A:HCG1332 2.5 5.3 1.0 CG A:ASP216 3.1 18.8 1.0 CE1 A:HIS214 3.2 14.3 1.0 CD2 A:HIS270 3.2 17.5 1.0 CD2 A:HIS214 3.3 16.1 1.0 CE1 A:HIS270 3.3 19.3 1.0 OD2 A:ASP216 3.4 16.9 1.0 C16 A:HCG1332 3.5 4.9 1.0 O A:HOH2073 3.9 35.9 1.0 ND1 A:HIS214 4.3 14.8 1.0 CG A:HIS270 4.4 16.4 1.0 ND1 A:HIS270 4.4 19.8 1.0 O A:HOH2217 4.4 30.5 1.0 CG A:HIS214 4.4 16.1 1.0 CB A:ASP216 4.5 18.1 1.0 O42 A:HCG1332 4.7 6.2 1.0 CA A:ASP216 4.8 17.6 1.0 O18 A:HCG1332 4.8 3.7 1.0 O A:HOH2190 4.8 31.0 1.0 C12 A:HCG1332 5.0 4.7 1.0 N A:ASP216 5.0 17.1 1.0

A.J.Long, I.J.Clifton, P.L.Roach, J.E.Baldwin, C.J.Schofield, P.J.Rutledge. Structural Studies on the Reaction of Isopenicillin N Synthase with the Truncated Substrate Analogues Delta-(L-Alpha-Aminoadipoyl)-L-Cysteinyl-Glycine and Delta-(L-Alpha-Aminoadipoyl)-L-Cysteinyl-D- Alanine Biochemistry V. 44 6619 2005.
ISSN: ISSN 0006-2960
PubMed: 15850395
DOI: 10.1021/BI047478Q