Iron in PDB 2vbp: Isopenicillin N Synthase with Substrate Analogue L,L,L-Acab (Unexposed)

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

The structure of Isopenicillin N Synthase with Substrate Analogue L,L,L-Acab (Unexposed), PDB code: 2vbp 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)	59.76 / 1.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	40.515, 74.340, 100.704, 90.00, 90.00, 90.00
R / Rfree (%)	14.7 / 18.1

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

Iron binding site 1 out of 1 in the Isopenicillin N Synthase with Substrate Analogue L,L,L-Acab (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,L-Acab (Unexposed) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1332 b:9.7 occ:1.00 O A:HOH2319 2.1 11.1 1.0 OD1 A:ASP216 2.2 10.8 1.0 O A:HOH2436 2.2 12.3 1.0 NE2 A:HIS270 2.2 8.0 1.0 NE2 A:HIS214 2.2 9.8 1.0 S17 A:VB11333 2.4 15.0 1.0 CE1 A:HIS270 3.1 8.9 1.0 CG A:ASP216 3.1 11.1 1.0 CE1 A:HIS214 3.2 10.6 1.0 CD2 A:HIS270 3.2 7.5 1.0 CD2 A:HIS214 3.2 9.3 1.0 C16 A:VB11333 3.4 19.2 1.0 OD2 A:ASP216 3.5 10.2 1.0 O A:HOH2001 3.9 25.8 1.0 O A:HOH2002 4.2 30.9 1.0 ND1 A:HIS270 4.3 8.2 1.0 O A:HOH2363 4.3 12.7 1.0 ND1 A:HIS214 4.3 9.6 1.0 CG A:HIS270 4.3 7.2 1.0 CG A:HIS214 4.4 10.4 1.0 O42 A:VB11333 4.4 31.2 1.0 CB A:ASP216 4.5 8.4 1.0 O A:HOH2320 4.7 16.4 1.0 CA A:ASP216 4.8 8.7 1.0 C12 A:VB11333 4.9 18.4 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