Iron in PDB 9eby: Crystal Structure of Rufo in Complex with Mrylh

The structure of Crystal Structure of Rufo in Complex with Mrylh, PDB code: 9eby was solved by K.Nolan, Y.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.28 / 2.03
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	55.163, 79.3, 88.511, 90, 90, 90
R / Rfree (%)	20.3 / 26.2

The binding sites of Iron atom in the Crystal Structure of Rufo in Complex with Mrylh (pdb code 9eby). 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 Rufo in Complex with Mrylh, PDB code: 9eby:

Iron binding site 1 out of 1 in the Crystal Structure of Rufo in Complex with Mrylh


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 Rufo in Complex with Mrylh within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:17.1 occ:1.00 FE A:HEM401 0.0 17.1 1.0 ND A:HEM401 2.0 19.5 1.0 NC A:HEM401 2.0 15.4 1.0 NB A:HEM401 2.1 15.5 1.0 NA A:HEM401 2.2 13.7 1.0 SG A:CYS346 2.3 15.9 1.0 O B:HOH101 2.6 17.0 0.7 C4C A:HEM401 3.0 15.6 1.0 C1D A:HEM401 3.0 15.7 1.0 C4D A:HEM401 3.0 22.3 1.0 C1C A:HEM401 3.0 17.5 1.0 C4B A:HEM401 3.1 17.3 1.0 C1A A:HEM401 3.1 15.8 1.0 C1B A:HEM401 3.2 16.2 1.0 C4A A:HEM401 3.2 14.8 1.0 CB A:CYS346 3.3 15.2 1.0 CHD A:HEM401 3.4 16.8 1.0 CHC A:HEM401 3.4 13.3 1.0 CHA A:HEM401 3.4 14.7 1.0 CHB A:HEM401 3.6 13.0 1.0 CA A:CYS346 3.9 19.1 1.0 C3C A:HEM401 4.2 18.5 1.0 C2D A:HEM401 4.2 18.2 1.0 C2C A:HEM401 4.2 15.5 1.0 C3D A:HEM401 4.3 15.8 1.0 C3B A:HEM401 4.3 13.1 1.0 C2B A:HEM401 4.4 14.1 1.0 C2A A:HEM401 4.4 17.4 1.0 C3A A:HEM401 4.4 16.4 1.0 OH B:TYR3 4.6 21.2 1.0 C A:CYS346 4.6 16.1 1.0 N A:LEU347 4.7 19.4 1.0 N A:GLY348 4.7 20.1 1.0 CB A:ALA236 5.0 14.5 1.0

K.Nolan, R.Usai, B.Li, S.Jordan, Y.Wang. Molecular Basis For Peptide Nitration By A Novel Cytochrome P450 Enzyme in Ripp Biosynthesis Acs Catalysis 10391 2025.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.5C01932