Iron in PDB 2vau: Isopenicillin N Synthase with Substrate Analogue Acomp ( Unexposed)

All present enzymatic activity of Isopenicillin N Synthase with Substrate Analogue Acomp ( Unexposed):
1.21.3.1;

The structure of Isopenicillin N Synthase with Substrate Analogue Acomp ( Unexposed), PDB code: 2vau 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)	30.41 / 1.8
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	46.697, 71.161, 100.912, 90.00, 90.00, 90.00
R / Rfree (%)	15.1 / 19

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

Iron binding site 1 out of 1 in the Isopenicillin N Synthase with Substrate Analogue Acomp ( 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 Acomp ( Unexposed) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1332 b:9.2 occ:1.00 OD1 A:ASP216 2.2 5.3 1.0 O A:HOH2247 2.2 7.9 1.0 NE2 A:HIS214 2.2 6.1 1.0 NE2 A:HIS270 2.3 4.5 1.0 SAI A:V201333 2.5 6.7 1.0 SAQ A:V201333 2.7 7.2 1.0 CG A:ASP216 3.1 7.3 1.0 CD2 A:HIS214 3.1 6.7 1.0 CE1 A:HIS270 3.2 6.7 1.0 CE1 A:HIS214 3.2 6.9 1.0 CD2 A:HIS270 3.3 8.2 1.0 OD2 A:ASP216 3.4 9.1 1.0 CAK A:V201333 3.5 7.0 1.0 CAN A:V201333 3.6 6.7 1.0 CAA A:V201333 3.8 11.0 1.0 O A:HOH2278 4.3 7.2 1.0 ND1 A:HIS270 4.3 5.7 1.0 CG A:HIS214 4.3 5.7 1.0 ND1 A:HIS214 4.3 4.1 1.0 CG A:HIS270 4.4 3.8 1.0 CB A:ASP216 4.4 7.4 1.0 OAP A:V201333 4.6 7.0 1.0 CA A:ASP216 4.7 6.6 1.0 CAW A:V201333 4.8 6.1 1.0 CAU A:V201333 4.8 8.1 1.0 CAX A:V201333 4.8 5.2 1.0 O A:HOH2249 4.9 7.0 1.0 N A:ASP216 5.0 7.3 1.0

W.Ge, I.J.Clifton, J.E.Stok, R.M.Adlington, J.E.Baldwin, P.J.Rutledge. Isopenicillin N Synthase Mediates Thiolate Oxidation to Sulfenate in A Depsipeptide Substrate Analogue: Implications For Oxygen Binding and A Link to Nitrile Hydratase? J.Am.Chem.Soc. V. 130 10096 2008.
ISSN: ISSN 0002-7863
PubMed: 18620394
DOI: 10.1021/JA8005397