Iron in PDB 2vbb: Isopenicillin N Synthase with Substrate Analogue Acomp ( 35MINUTES Oxygen Exposure)

All present enzymatic activity of Isopenicillin N Synthase with Substrate Analogue Acomp ( 35MINUTES Oxygen Exposure):
1.21.3.1;

The structure of Isopenicillin N Synthase with Substrate Analogue Acomp ( 35MINUTES Oxygen Exposure), PDB code: 2vbb 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)	58.03 / 1.4
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	46.655, 71.041, 100.763, 90.00, 90.00, 90.00
R / Rfree (%)	15.1 / 17.2

The binding sites of Iron atom in the Isopenicillin N Synthase with Substrate Analogue Acomp ( 35MINUTES Oxygen Exposure) (pdb code 2vbb). 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 ( 35MINUTES Oxygen Exposure), PDB code: 2vbb:

Iron binding site 1 out of 1 in the Isopenicillin N Synthase with Substrate Analogue Acomp ( 35MINUTES Oxygen Exposure)


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 ( 35MINUTES Oxygen Exposure) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1333 b:9.0 occ:1.00 OAG A:VAZ1332 2.1 17.0 0.7 OD1 A:ASP216 2.1 6.9 1.0 O A:HOH2314 2.1 12.3 1.0 NE2 A:HIS214 2.2 5.4 1.0 NE2 A:HIS270 2.2 5.2 1.0 SAR A:VAZ1332 2.4 14.2 0.7 SAQ A:VAZ1332 2.5 14.9 0.7 CG A:ASP216 3.1 7.3 1.0 CE1 A:HIS270 3.1 5.3 1.0 CD2 A:HIS214 3.2 5.4 1.0 CE1 A:HIS214 3.2 5.2 1.0 CD2 A:HIS270 3.2 5.5 1.0 CAY A:VAZ1332 3.4 22.9 0.7 OD2 A:ASP216 3.4 5.9 1.0 CAN A:VAZ1332 3.5 17.9 0.7 CAA A:VAZ1332 3.7 9.6 0.3 OAJ A:VAZ1332 4.1 26.1 0.7 CAA A:VAZ1332 4.1 17.4 0.3 ND1 A:HIS270 4.3 5.6 1.0 O A:HOH2358 4.3 15.7 1.0 ND1 A:HIS214 4.3 5.4 1.0 CG A:HIS214 4.3 5.3 1.0 CG A:HIS270 4.3 4.9 1.0 CB A:ASP216 4.4 5.5 1.0 OAP A:VAZ1332 4.5 17.7 0.7 CAX A:VAZ1332 4.7 14.3 0.7 CAV A:VAZ1332 4.7 12.4 0.7 CA A:ASP216 4.8 5.5 1.0 CAZ A:VAZ1332 4.8 17.1 0.7 N A:ASP216 4.9 5.3 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