Iron in PDB 2bjs: Isopenicillin N Synthase C-Terminal Truncation Mutant

All present enzymatic activity of Isopenicillin N Synthase C-Terminal Truncation Mutant:
1.21.3.1;

The structure of Isopenicillin N Synthase C-Terminal Truncation Mutant, PDB code: 2bjs was solved by L.A.Mcneill, M.Sami, I.J.Clifton, N.I.Burzlaff, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	58.12 / 1.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	47.149, 71.126, 100.991, 90.00, 90.00, 90.00
R / Rfree (%)	13.9 / 16.4

The binding sites of Iron atom in the Isopenicillin N Synthase C-Terminal Truncation Mutant (pdb code 2bjs). 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 C-Terminal Truncation Mutant, PDB code: 2bjs:

Iron binding site 1 out of 1 in the Isopenicillin N Synthase C-Terminal Truncation Mutant


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 C-Terminal Truncation Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1323 b:9.4 occ:1.00 O A:HOH2408 2.0 15.8 1.0 OD1 A:ASP216 2.1 18.3 1.0 NE2 A:HIS214 2.1 16.7 1.0 NE2 A:HIS270 2.4 19.5 1.0 S17 A:ACV1324 2.4 5.7 0.5 O A:HOH2402 2.6 14.8 0.5 CG A:ASP216 3.1 17.9 1.0 CD2 A:HIS214 3.1 15.4 1.0 CE1 A:HIS214 3.2 17.4 1.0 CE1 A:HIS270 3.2 17.9 1.0 OD2 A:ASP216 3.4 17.4 1.0 CD2 A:HIS270 3.4 18.6 1.0 C16 A:ACV1324 3.5 5.6 0.5 C33 A:ACV1324 3.8 15.2 0.5 C37 A:ACV1324 3.9 11.5 0.5 C32 A:ACV1324 4.0 11.7 0.5 C37 A:ACV1324 4.2 12.0 0.5 O A:HOH2457 4.2 17.9 1.0 ND1 A:HIS214 4.3 17.3 1.0 CG A:HIS214 4.3 16.8 1.0 ND1 A:HIS270 4.4 16.6 1.0 CB A:ASP216 4.4 16.7 1.0 CG A:HIS270 4.5 17.1 1.0 C32 A:ACV1324 4.5 14.8 0.5 CA A:ASP216 4.6 16.8 1.0 C12 A:ACV1324 4.7 3.6 0.5 C13 A:ACV1324 4.8 3.1 0.5 N A:ASP216 4.8 16.1 1.0 N29 A:ACV1324 4.8 4.8 0.5 C33 A:ACV1324 4.8 8.7 0.5 O A:HOH2410 4.9 13.3 1.0

L.A.Mcneill, T.J.N.Brown, M.Sami, I.J.Clifton, N.I.Burzlaff, T.D.W.Claridge, R.M.Adlington, J.E.Baldwin, P.J.Rutledge, C.J.Schofield. Terminally Truncated Isopenicillin N Synthase Generates A Dithioester Product: Evidence For A Thioaldehyde Intermediate During Catalysis and A New Mode of Reaction For Non-Heme Iron Oxidases. Chemistry V. 23 12815 2017.
ISSN: ISSN 1521-3765
PubMed: 28703303
DOI: 10.1002/CHEM.201701592