Iron in PDB 1uzw: Isopenicillin N Synthase with L-D-(A-Aminoadipoyl)-L-Cysteinyl-D-Isodehydrovaline

All present enzymatic activity of Isopenicillin N Synthase with L-D-(A-Aminoadipoyl)-L-Cysteinyl-D-Isodehydrovaline:
1.21.3.1;

The structure of Isopenicillin N Synthase with L-D-(A-Aminoadipoyl)-L-Cysteinyl-D-Isodehydrovaline, PDB code: 1uzw was solved by A.R.Grummitt, P.J.Rutledge, I.J.Clifton, J.E.Baldwin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	57.74 / 1.3
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	46.228, 70.595, 100.639, 90.00, 90.00, 90.00
R / Rfree (%)	17.3 / 19.4

The binding sites of Iron atom in the Isopenicillin N Synthase with L-D-(A-Aminoadipoyl)-L-Cysteinyl-D-Isodehydrovaline (pdb code 1uzw). 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 with L-D-(A-Aminoadipoyl)-L-Cysteinyl-D-Isodehydrovaline, PDB code: 1uzw:

Iron binding site 1 out of 1 in the Isopenicillin N Synthase with L-D-(A-Aminoadipoyl)-L-Cysteinyl-D-Isodehydrovaline


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 with L-D-(A-Aminoadipoyl)-L-Cysteinyl-D-Isodehydrovaline within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1332 b:9.2 occ:1.00 O A:HOH2260 1.7 11.9 1.0 OD1 A:ASP216 2.0 9.6 1.0 NE2 A:HIS270 2.0 8.3 1.0 NE2 A:HIS214 2.3 5.1 1.0 O A:HOH2255 2.3 10.5 1.0 S A:CDH1333 2.4 4.8 0.3 S A:CDH1333 2.4 26.6 0.7 CG A:ASP216 2.9 7.5 1.0 CE1 A:HIS270 2.9 6.6 1.0 CD2 A:HIS270 3.1 6.9 1.0 OD2 A:ASP216 3.2 7.4 1.0 CD2 A:HIS214 3.2 7.0 1.0 CE1 A:HIS214 3.3 8.8 1.0 C16 A:CDH1333 3.6 7.8 0.3 C16 A:CDH1333 3.6 32.2 0.7 C33 A:CDH1333 3.9 8.8 0.3 ND1 A:HIS270 4.1 6.9 1.0 O A:HOH2291 4.1 17.3 1.0 CG A:HIS270 4.2 6.5 1.0 CB A:ASP216 4.3 6.8 1.0 CG A:HIS214 4.4 7.2 1.0 ND1 A:HIS214 4.4 8.4 1.0 C33 A:CDH1333 4.4 41.2 0.7 N29 A:CDH1333 4.6 38.8 0.7 C32 A:CDH1333 4.6 12.8 0.3 CA A:ASP216 4.7 7.4 1.0 C32 A:CDH1333 4.8 42.3 0.7 N A:ASP216 4.8 6.3 1.0 C12 A:CDH1333 4.9 7.4 0.3 N29 A:CDH1333 4.9 7.8 0.3 O A:HOH2261 5.0 19.3 1.0

A.R.Grummitt, P.J.Rutledge, I.J.Clifton, J.E.Baldwin. Active Site Mediated Elimination of Hydrogen Fluoride From A Fluorinated Substrate Analogue By Isopenicillin N Synthase Biochem.J. V. 382 659 2004.
ISSN: ISSN 0264-6021
PubMed: 15175003
DOI: 10.1042/BJ20040529