Iron in PDB 8fic: Crystal Structure of Erwinia Tracheiphila CYP114 in Complex with Ent- Kaurenoic Acid (Crystal Form 1)

The structure of Crystal Structure of Erwinia Tracheiphila CYP114 in Complex with Ent- Kaurenoic Acid (Crystal Form 1), PDB code: 8fic was solved by C.E.Stewart Jr., R.Nagel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	59.34 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.82, 70.46, 110.04, 90, 90, 90
R / Rfree (%)	16 / 18.9

The binding sites of Iron atom in the Crystal Structure of Erwinia Tracheiphila CYP114 in Complex with Ent- Kaurenoic Acid (Crystal Form 1) (pdb code 8fic). 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 Crystal Structure of Erwinia Tracheiphila CYP114 in Complex with Ent- Kaurenoic Acid (Crystal Form 1), PDB code: 8fic:

Iron binding site 1 out of 1 in the Crystal Structure of Erwinia Tracheiphila CYP114 in Complex with Ent- Kaurenoic Acid (Crystal Form 1)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Erwinia Tracheiphila CYP114 in Complex with Ent- Kaurenoic Acid (Crystal Form 1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:18.6 occ:1.00 FE A:HEM500 0.0 18.6 1.0 ND A:HEM500 2.0 18.2 1.0 NC A:HEM500 2.0 18.5 1.0 NB A:HEM500 2.1 17.4 1.0 NA A:HEM500 2.1 17.4 1.0 SG A:CYS380 2.4 17.2 1.0 C4B A:HEM500 3.0 18.9 1.0 C1C A:HEM500 3.0 18.9 1.0 C1D A:HEM500 3.0 19.8 1.0 C1B A:HEM500 3.1 18.0 1.0 C4C A:HEM500 3.1 18.8 1.0 C4A A:HEM500 3.1 16.2 1.0 C4D A:HEM500 3.1 17.4 1.0 C1A A:HEM500 3.1 16.8 1.0 HB2 A:CYS380 3.2 20.1 1.0 CB A:CYS380 3.4 16.8 1.0 CHC A:HEM500 3.4 20.4 1.0 CHD A:HEM500 3.4 19.2 1.0 CHB A:HEM500 3.4 17.6 1.0 CHA A:HEM500 3.5 16.7 1.0 HA A:CYS380 3.5 19.6 1.0 H A:GLY382 3.6 22.1 1.0 H092 A:NE4501 3.8 28.0 1.0 O A:HOH654 3.9 22.9 1.0 CA A:CYS380 3.9 16.3 1.0 H082 A:NE4501 4.0 26.5 1.0 H091 A:NE4501 4.0 28.0 1.0 H A:LEU381 4.1 21.7 1.0 HB3 A:CYS380 4.2 20.1 1.0 C3B A:HEM500 4.2 18.0 1.0 C2B A:HEM500 4.3 18.7 1.0 C2C A:HEM500 4.3 19.2 1.0 HD1 A:PHE373 4.3 21.6 1.0 C2D A:HEM500 4.3 19.1 1.0 C3C A:HEM500 4.3 21.1 1.0 C3A A:HEM500 4.3 15.8 1.0 C3D A:HEM500 4.3 18.0 1.0 C2A A:HEM500 4.3 15.4 1.0 C09 A:NE4501 4.3 23.3 1.0 HHC A:HEM500 4.4 24.5 1.0 HHD A:HEM500 4.4 23.0 1.0 HHB A:HEM500 4.4 21.2 1.0 HHA A:HEM500 4.4 20.0 1.0 N A:GLY382 4.5 18.4 1.0 N A:LEU381 4.5 18.1 1.0 C A:CYS380 4.6 16.8 1.0 C08 A:NE4501 4.6 22.1 1.0 HA3 A:GLY382 4.6 22.9 1.0 HG1 A:THR262 4.7 30.0 1.0 H193 A:NE4501 4.9 25.2 1.0 H192 A:NE4501 5.0 25.2 1.0

R.Nagel, L.E.Alexander, C.E.Stewart Jr., R.J.Peters. Dual Factors Required For Cytochrome-P450-Mediated Hydrocarbon Ring Contraction in Bacterial Gibberellin Phytohormone Biosynthesis. Proc.Natl.Acad.Sci.Usa V. 120 49120 2023.
ISSN: ESSN 1091-6490
PubMed: 37339230
DOI: 10.1073/PNAS.2221549120