Iron in PDB 9g9q: Crystal Structure of Pbda Bound to P-Methoxybenzoate.

The structure of Crystal Structure of Pbda Bound to P-Methoxybenzoate., PDB code: 9g9q 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)	52.60 / 2.03
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	52.17, 55.11, 64.26, 99.87, 94.9, 103.24
R / Rfree (%)	16.4 / 25.8

The binding sites of Iron atom in the Crystal Structure of Pbda Bound to P-Methoxybenzoate. (pdb code 9g9q). 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 P-Methoxybenzoate., PDB code: 9g9q:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Pbda Bound to P-Methoxybenzoate.


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 P-Methoxybenzoate. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:22.3 occ:1.00 FE A:HEM501 0.0 22.3 1.0 ND A:HEM501 1.9 22.5 1.0 NA A:HEM501 2.0 19.0 1.0 NB A:HEM501 2.1 21.9 1.0 NC A:HEM501 2.1 23.7 1.0 SG A:CYS349 2.3 21.6 1.0 C4D A:HEM501 2.9 19.0 1.0 C1D A:HEM501 3.0 21.7 1.0 C1A A:HEM501 3.0 19.3 1.0 C4B A:HEM501 3.0 22.5 1.0 C4A A:HEM501 3.0 21.6 1.0 C1B A:HEM501 3.0 19.5 1.0 C1C A:HEM501 3.1 23.7 1.0 C4C A:HEM501 3.1 24.3 1.0 HB2 A:CYS349 3.1 22.2 1.0 H83 A:ANN502 3.2 21.7 1.0 CB A:CYS349 3.3 22.3 1.0 CHA A:HEM501 3.3 18.4 1.0 CHB A:HEM501 3.4 20.2 1.0 CHC A:HEM501 3.4 25.3 1.0 CHD A:HEM501 3.5 22.0 1.0 HA A:CYS349 3.5 21.6 1.0 H A:GLY351 3.9 23.5 1.0 HB3 A:ALA239 3.9 24.1 1.0 CA A:CYS349 4.0 21.4 1.0 C8 A:ANN502 4.1 21.9 1.0 HB3 A:CYS349 4.1 22.0 1.0 C3D A:HEM501 4.2 21.8 1.0 C2D A:HEM501 4.2 22.1 1.0 C3B A:HEM501 4.2 20.9 1.0 HG21 A:THR243 4.3 26.2 1.0 C2B A:HEM501 4.3 20.4 1.0 C2C A:HEM501 4.3 23.0 1.0 C3C A:HEM501 4.3 24.2 1.0 C2A A:HEM501 4.3 20.8 1.0 HHA A:HEM501 4.3 18.5 1.0 H81 A:ANN502 4.3 22.0 1.0 C3A A:HEM501 4.3 22.5 1.0 H6 A:ANN502 4.3 22.9 1.0 HHB A:HEM501 4.4 20.2 1.0 H A:VAL350 4.4 22.8 1.0 HD1 A:TYR342 4.4 21.3 1.0 HHC A:HEM501 4.4 24.3 1.0 H82 A:ANN502 4.4 21.5 1.0 HHD A:HEM501 4.4 22.1 1.0 HA3 A:GLY351 4.7 22.6 1.0 C A:CYS349 4.7 21.6 1.0 N A:GLY351 4.7 23.4 1.0 N A:VAL350 4.8 23.2 1.0 CB A:ALA239 4.9 24.0 1.0 O A:ALA239 4.9 28.1 1.0 C6 A:ANN502 5.0 22.7 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Pbda Bound to P-Methoxybenzoate.


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 P-Methoxybenzoate. within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:21.6 occ:1.00 FE B:HEM501 0.0 21.6 1.0 ND B:HEM501 1.9 21.1 1.0 NA B:HEM501 2.0 19.1 1.0 NB B:HEM501 2.1 20.6 1.0 NC B:HEM501 2.1 22.9 1.0 SG B:CYS349 2.3 20.1 1.0 C4D B:HEM501 2.9 20.5 1.0 C1D B:HEM501 2.9 21.3 1.0 C1A B:HEM501 3.0 20.1 1.0 C4B B:HEM501 3.0 21.0 1.0 C4C B:HEM501 3.0 22.1 1.0 C4A B:HEM501 3.0 21.2 1.0 C1B B:HEM501 3.1 20.6 1.0 C1C B:HEM501 3.2 20.4 1.0 HB2 B:CYS349 3.2 20.1 1.0 CHD B:HEM501 3.3 21.9 1.0 CB B:CYS349 3.3 20.4 1.0 H83 B:ANN502 3.4 22.9 1.0 CHA B:HEM501 3.4 19.9 1.0 HA B:CYS349 3.4 19.2 1.0 CHC B:HEM501 3.4 20.5 1.0 CHB B:HEM501 3.5 19.4 1.0 H B:GLY351 3.9 24.9 1.0 HB3 B:ALA239 3.9 18.9 1.0 CA B:CYS349 3.9 19.1 1.0 HB3 B:CYS349 4.2 20.0 1.0 HG21 B:THR243 4.2 22.9 1.0 C3D B:HEM501 4.2 21.0 1.0 C2A B:HEM501 4.2 19.9 1.0 C2D B:HEM501 4.2 21.9 1.0 C3A B:HEM501 4.3 22.0 1.0 C3B B:HEM501 4.3 20.9 1.0 C3C B:HEM501 4.3 20.7 1.0 HHD B:HEM501 4.3 21.6 1.0 C8 B:ANN502 4.3 22.8 1.0 HHA B:HEM501 4.3 20.3 1.0 C2B B:HEM501 4.3 20.7 1.0 C2C B:HEM501 4.4 19.4 1.0 H4 B:ANN502 4.4 25.4 1.0 HHC B:HEM501 4.4 20.6 1.0 HD1 B:TYR342 4.4 22.4 1.0 HHB B:HEM501 4.4 20.2 1.0 H B:VAL350 4.5 21.8 1.0 H82 B:ANN502 4.6 22.7 1.0 HA3 B:GLY351 4.6 25.3 1.0 H81 B:ANN502 4.7 22.9 1.0 N B:GLY351 4.7 25.0 1.0 C B:CYS349 4.7 19.7 1.0 CB B:ALA239 4.8 18.5 1.0 O B:ALA239 4.8 26.2 1.0 N B:VAL350 4.8 21.6 1.0 HB2 B:ALA239 4.9 19.1 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