Iron in PDB 2wo7: Isopenicillin N Synthase with Substrate Analogue L,L,D- ACD2AB (Unexposed)

All present enzymatic activity of Isopenicillin N Synthase with Substrate Analogue L,L,D- ACD2AB (Unexposed):
1.21.3.1;

The structure of Isopenicillin N Synthase with Substrate Analogue L,L,D- ACD2AB (Unexposed), PDB code: 2wo7 was solved by W.Ge, I.J.Clifton, R.M.Adlington, J.E.Baldwin, P.J.Rutledge, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	60.75 / 2.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	41.484, 75.935, 101.016, 90.00, 90.00, 90.00
R / Rfree (%)	18.605 / 25.684

The binding sites of Iron atom in the Isopenicillin N Synthase with Substrate Analogue L,L,D- ACD2AB (Unexposed) (pdb code 2wo7). 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 Substrate Analogue L,L,D- ACD2AB (Unexposed), PDB code: 2wo7:

Iron binding site 1 out of 1 in the Isopenicillin N Synthase with Substrate Analogue L,L,D- ACD2AB (Unexposed)


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 Substrate Analogue L,L,D- ACD2AB (Unexposed) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1332 b:11.1 occ:1.00 OD1 A:ASP216 2.2 11.7 1.0 NE2 A:HIS214 2.2 9.1 1.0 O A:HOH2300 2.3 13.7 1.0 NE2 A:HIS270 2.3 8.0 1.0 O A:HOH2216 2.3 10.0 1.0 S17 A:ASV1333 2.4 16.8 1.0 CD2 A:HIS214 3.1 8.0 1.0 CD2 A:HIS270 3.2 7.9 1.0 CG A:ASP216 3.2 9.4 1.0 CE1 A:HIS214 3.3 10.2 1.0 CE1 A:HIS270 3.3 6.8 1.0 C16 A:ASV1333 3.3 17.0 1.0 OD2 A:ASP216 3.6 9.1 1.0 C33 A:ASV1333 3.8 21.8 1.0 O A:HOH2249 4.1 15.9 1.0 N29 A:ASV1333 4.2 23.2 1.0 CG A:HIS214 4.3 8.9 1.0 CG A:HIS270 4.3 7.6 1.0 ND1 A:HIS214 4.3 10.3 1.0 ND1 A:HIS270 4.4 7.1 1.0 C32 A:ASV1333 4.5 22.9 1.0 CB A:ASP216 4.5 8.2 1.0 O A:HOH2217 4.6 15.8 1.0 C12 A:ASV1333 4.7 19.8 1.0 CA A:ASP216 4.8 8.6 1.0 C13 A:ASV1333 4.9 23.5 1.0 N A:ASP216 5.0 9.2 1.0 C30 A:ASV1333 5.0 23.2 1.0

W.Ge, I.J.Clifton, J.E.Stok, R.M.Adlington, J.E.Baldwin, P.J.Rutledge. Crystallographic Studies on the Binding of Selectively Deuterated Lld- and Lll-Substrate Epimers By Isopenicillin N Synthase. Biochem.Biophys.Res.Commun. V. 398 659 2010.
ISSN: ISSN 0006-291X
PubMed: 20603104
DOI: 10.1016/J.BBRC.2010.06.129