Iron in PDB 4bb3: Isopenicillin N Synthase with the Dipeptide Substrate Analogue Ahc

All present enzymatic activity of Isopenicillin N Synthase with the Dipeptide Substrate Analogue Ahc:
1.21.3.1;

The structure of Isopenicillin N Synthase with the Dipeptide Substrate Analogue Ahc, PDB code: 4bb3 was solved by A.Daruzzaman, 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)	58.28 / 1.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	46.508, 71.202, 100.884, 90.00, 90.00, 90.00
R / Rfree (%)	17.2 / 18.8

The binding sites of Iron atom in the Isopenicillin N Synthase with the Dipeptide Substrate Analogue Ahc (pdb code 4bb3). 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 the Dipeptide Substrate Analogue Ahc, PDB code: 4bb3:

Iron binding site 1 out of 1 in the Isopenicillin N Synthase with the Dipeptide Substrate Analogue Ahc


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 the Dipeptide Substrate Analogue Ahc within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1332 b:9.5 occ:1.00 OD1 A:ASP216 2.1 9.2 1.0 NE2 A:HIS214 2.1 9.0 1.0 O A:HOH2211 2.1 15.0 1.0 NE2 A:HIS270 2.2 8.9 1.0 O A:HOH2203 2.2 13.2 1.0 O1 A:KKA1333 2.3 15.4 1.0 C8 A:KKA1333 3.1 20.1 1.0 CE1 A:HIS214 3.1 9.2 1.0 CG A:ASP216 3.1 8.8 1.0 CE1 A:HIS270 3.1 9.0 1.0 CD2 A:HIS214 3.1 9.4 1.0 CD2 A:HIS270 3.2 8.8 1.0 OD2 A:ASP216 3.4 8.4 1.0 O2 A:KKA1333 3.4 20.4 1.0 O A:HOH2237 4.1 30.4 1.0 ND1 A:HIS214 4.3 9.8 1.0 ND1 A:HIS270 4.3 8.6 1.0 CG A:HIS214 4.3 9.3 1.0 CG A:HIS270 4.3 8.8 1.0 C5 A:KKA1333 4.5 22.3 1.0 CB A:ASP216 4.5 8.4 1.0 O A:HOH2212 4.5 17.0 1.0 CA A:ASP216 4.8 8.7 1.0 C6 A:KKA1333 4.9 24.7 1.0 N1 A:KKA1333 4.9 21.2 1.0 N A:ASP216 4.9 8.9 1.0

A.Daruzzaman, I.J.Clifton, R.M.Adlington, J.E.Baldwin, P.J.Rutledge. The Crystal Structure of Isopenicillin N Synthase with A Dipeptide Substrate Analogue. Arch.Biochem.Biophys. V. 530 48 2013.
ISSN: ISSN 0003-9861
PubMed: 23262315
DOI: 10.1016/J.ABB.2012.12.012