Iron in PDB 9g9s: Crystal Structure of Pbda Bound to Veratrate

The structure of Crystal Structure of Pbda Bound to Veratrate, PDB code: 9g9s was solved by D.J.Hinchen, M.E.Wolf, L.D.Eltis, J.E.Mcgeehan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	63.54 / 1.85
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	50.999, 55.357, 64.693, 98.68, 95, 99.01
R / Rfree (%)	20.8 / 25.8

The binding sites of Iron atom in the Crystal Structure of Pbda Bound to Veratrate (pdb code 9g9s). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Pbda Bound to Veratrate, PDB code: 9g9s:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Pbda Bound to Veratrate


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 Pbda Bound to Veratrate within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:17.7 occ:1.00 FE A:HEM501 0.0 17.7 1.0 ND A:HEM501 1.9 18.0 1.0 NA A:HEM501 2.0 18.9 1.0 NB A:HEM501 2.1 16.1 1.0 NC A:HEM501 2.1 17.4 1.0 SG A:CYS349 2.4 18.1 1.0 C1D A:HEM501 3.0 17.6 1.0 C4D A:HEM501 3.0 18.4 1.0 C4A A:HEM501 3.0 19.2 1.0 C1A A:HEM501 3.0 19.4 1.0 C1B A:HEM501 3.0 17.8 1.0 C4B A:HEM501 3.0 17.3 1.0 C4C A:HEM501 3.0 16.4 1.0 C1C A:HEM501 3.1 17.4 1.0 HB2 A:CYS349 3.3 16.7 1.0 H8 A:TWO502 3.3 21.2 1.0 CHB A:HEM501 3.4 18.6 1.0 CB A:CYS349 3.4 16.8 1.0 CHD A:HEM501 3.4 18.4 1.0 CHA A:HEM501 3.4 18.6 1.0 CHC A:HEM501 3.5 18.2 1.0 HA A:CYS349 3.5 15.5 1.0 H A:GLY351 3.9 17.9 1.0 CA A:CYS349 4.0 15.4 1.0 HB3 A:ALA239 4.0 28.0 1.0 HG21 A:THR243 4.1 23.0 1.0 C8 A:TWO502 4.1 21.1 1.0 C3A A:HEM501 4.2 19.6 1.0 C2A A:HEM501 4.2 19.8 1.0 C2D A:HEM501 4.2 17.8 1.0 HB3 A:CYS349 4.2 16.7 1.0 C3D A:HEM501 4.2 17.5 1.0 C3C A:HEM501 4.2 16.9 1.0 C3B A:HEM501 4.3 18.8 1.0 C2B A:HEM501 4.3 17.4 1.0 H7 A:TWO502 4.3 21.2 1.0 C2C A:HEM501 4.3 19.0 1.0 HHB A:HEM501 4.3 18.6 1.0 HHD A:HEM501 4.4 17.8 1.0 H6 A:TWO502 4.4 21.2 1.0 HHA A:HEM501 4.4 18.7 1.0 HHC A:HEM501 4.4 17.9 1.0 HA3 A:GLY351 4.5 19.2 1.0 H9 A:TWO502 4.5 20.9 1.0 HD1 A:TYR342 4.5 21.3 1.0 H A:VAL350 4.5 16.1 1.0 N A:GLY351 4.7 17.8 1.0 C A:CYS349 4.7 15.9 1.0 N A:VAL350 4.9 15.1 1.0 CB A:ALA239 5.0 28.3 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Pbda Bound to Veratrate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Pbda Bound to Veratrate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:18.4 occ:1.00 FE B:HEM501 0.0 18.4 1.0 ND B:HEM501 1.9 17.2 1.0 NA B:HEM501 2.0 16.6 1.0 NC B:HEM501 2.1 19.1 1.0 NB B:HEM501 2.1 19.7 1.0 SG B:CYS349 2.3 18.3 1.0 HG B:CYS349 2.6 18.2 0.0 C1D B:HEM501 2.9 18.1 1.0 C4D B:HEM501 3.0 17.6 1.0 C1A B:HEM501 3.0 16.3 1.0 C4B B:HEM501 3.0 21.6 1.0 C4A B:HEM501 3.0 18.5 1.0 C4C B:HEM501 3.0 16.7 1.0 C1B B:HEM501 3.1 20.2 1.0 C1C B:HEM501 3.1 19.3 1.0 HB2 B:CYS349 3.2 17.6 1.0 H8 B:TWO502 3.3 20.6 1.0 CB B:CYS349 3.4 17.3 1.0 CHD B:HEM501 3.4 17.1 1.0 CHA B:HEM501 3.4 17.6 1.0 CHC B:HEM501 3.4 21.6 1.0 CHB B:HEM501 3.4 19.5 1.0 HA B:CYS349 3.6 17.9 1.0 HB3 B:ALA239 3.8 17.6 1.0 H B:GLY351 4.0 19.6 1.0 CA B:CYS349 4.0 17.8 1.0 C8 B:TWO502 4.2 20.9 1.0 HB3 B:CYS349 4.2 17.6 1.0 C2D B:HEM501 4.2 20.7 1.0 C2A B:HEM501 4.2 17.3 1.0 C3D B:HEM501 4.2 18.6 1.0 C3C B:HEM501 4.2 16.8 1.0 C3A B:HEM501 4.2 18.0 1.0 HG21 B:THR243 4.2 21.1 1.0 C3B B:HEM501 4.3 22.3 1.0 C2B B:HEM501 4.3 20.9 1.0 C2C B:HEM501 4.3 18.9 1.0 H9 B:TWO502 4.3 16.6 1.0 HHD B:HEM501 4.4 17.4 1.0 HHA B:HEM501 4.4 17.3 1.0 HHC B:HEM501 4.4 21.0 1.0 O B:ALA239 4.4 22.0 1.0 HHB B:HEM501 4.4 19.4 1.0 HD1 B:TYR342 4.4 18.1 1.0 H6 B:TWO502 4.4 20.6 1.0 H7 B:TWO502 4.4 20.7 1.0 HA3 B:GLY351 4.6 19.7 1.0 H B:VAL350 4.7 18.9 1.0 CB B:ALA239 4.7 17.3 1.0 C B:CYS349 4.7 19.3 1.0 N B:GLY351 4.8 18.7 1.0 HB2 B:ALA239 4.8 17.6 1.0 N B:VAL350 5.0 18.0 1.0 C1 B:TWO502 5.0 15.4 1.0

M.E.Wolf, D.J.Hinchen, J.E.Mcgeehan, L.D.Eltis. Characterization of A Cytochrome P450 That Catalyzes the O-Demethylation of Lignin-Derived Benzoates. J.Biol.Chem. 07809 2024.
ISSN: ESSN 1083-351X
PubMed: 39307304
DOI: 10.1016/J.JBC.2024.107809