Iron in PDB 7poy: Spin Labeled Ipns S55C Variant in Complex with Fe, Acv and No

All present enzymatic activity of Spin Labeled Ipns S55C Variant in Complex with Fe, Acv and No:
1.21.3.1;

The structure of Spin Labeled Ipns S55C Variant in Complex with Fe, Acv and No, PDB code: 7poy was solved by P.Rabe, I.Clifton, C.Walla, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.88 / 1.75
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	41.374, 74.907, 101.048, 90, 90, 90
R / Rfree (%)	18.1 / 21.7

The binding sites of Iron atom in the Spin Labeled Ipns S55C Variant in Complex with Fe, Acv and No (pdb code 7poy). 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 Spin Labeled Ipns S55C Variant in Complex with Fe, Acv and No, PDB code: 7poy:

Iron binding site 1 out of 1 in the Spin Labeled Ipns S55C Variant in Complex with Fe, Acv and No


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Spin Labeled Ipns S55C Variant in Complex with Fe, Acv and No within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:20.2 occ:1.00 OD1 A:ASP216 2.0 19.9 1.0 O A:HOH547 2.1 24.2 1.0 NE2 A:HIS214 2.2 17.8 1.0 N A:NO403 2.2 29.8 0.8 S17 A:ACV402 2.3 23.2 1.0 NE2 A:HIS270 2.3 18.0 1.0 CG A:ASP216 2.9 20.3 1.0 CD2 A:HIS214 3.1 20.4 1.0 CE1 A:HIS270 3.2 15.9 1.0 O A:NO403 3.2 34.5 0.8 HD2 A:HIS214 3.2 24.5 1.0 CE1 A:HIS214 3.2 20.3 1.0 CD2 A:HIS270 3.2 18.7 1.0 OD2 A:ASP216 3.3 20.5 1.0 HE1 A:HIS270 3.3 19.1 1.0 C16 A:ACV402 3.3 27.1 1.0 HE1 A:HIS214 3.4 24.4 1.0 HD2 A:HIS270 3.4 22.4 1.0 C33 A:ACV402 3.9 26.5 0.2 O A:HOH665 3.9 26.2 1.0 C37 A:ACV402 4.1 26.7 0.8 HA A:ASP216 4.1 21.0 1.0 C37 A:ACV402 4.2 26.7 0.2 CG A:HIS214 4.2 20.1 1.0 ND1 A:HIS270 4.3 15.6 1.0 ND1 A:HIS214 4.3 18.6 1.0 CB A:ASP216 4.3 18.7 1.0 HE1 A:PHE285 4.3 24.8 1.0 CG A:HIS270 4.3 18.4 1.0 CA A:ASP216 4.6 17.5 1.0 C32 A:ACV402 4.6 28.8 0.2 C12 A:ACV402 4.7 25.6 0.8 C12 A:ACV402 4.7 25.8 0.2 O A:HOH647 4.7 24.1 1.0 N29 A:ACV402 4.7 27.0 0.2 C33 A:ACV402 4.7 30.3 0.8 HB3 A:ASP216 4.7 22.4 1.0 HG21 A:THR221 4.7 19.4 1.0 N29 A:ACV402 4.8 26.9 0.8 C13 A:ACV402 4.8 29.6 0.8 N A:ASP216 4.8 18.2 1.0 C13 A:ACV402 4.8 29.4 0.2 HE2 A:PHE211 4.9 34.2 1.0 HB2 A:ASP216 4.9 22.4 1.0 HG1 A:THR221 4.9 19.4 1.0 H A:ASP216 4.9 21.8 1.0 C32 A:ACV402 5.0 29.2 0.8 HD21 A:ASN252 5.0 20.6 1.0

P.Rabe, C.C.Walla, N.K.Goodyear, J.Welsh, R.Southwart, I.Clifton, J.D.S.Linyard, A.Tumber, T.D.W.Claridge, W.K.Myers, C.J.Schofield. Spectroscopic Studies Reveal Details of Substrate-Induced Conformational Changes Distant From the Active Site in Isopenicillin N Synthase. J.Biol.Chem. V. 298 02249 2022.
ISSN: ESSN 1083-351X
PubMed: 35835215
DOI: 10.1016/J.JBC.2022.102249