Iron in PDB 6g5q: The Structure of A Carbohydrate Active P450

The structure of The Structure of A Carbohydrate Active P450, PDB code: 6g5q was solved by C.S.Robb, J.H.Hehemann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	99.83 / 2.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	63.024, 67.878, 199.653, 90.00, 90.00, 90.00
R / Rfree (%)	17.2 / 21.7

The binding sites of Iron atom in the The Structure of A Carbohydrate Active P450 (pdb code 6g5q). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the The Structure of A Carbohydrate Active P450, PDB code: 6g5q:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the The Structure of A Carbohydrate Active P450


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Structure of A Carbohydrate Active P450 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe402 b:23.3 occ:1.00 FE A:HEM402 0.0 23.3 1.0 ND A:HEM402 1.9 20.5 1.0 NA A:HEM402 2.0 19.9 1.0 NC A:HEM402 2.1 20.1 1.0 NB A:HEM402 2.1 20.2 1.0 SG A:CYS330 2.4 23.2 1.0 C1D A:HEM402 2.9 19.9 1.0 C4D A:HEM402 2.9 19.9 1.0 C4C A:HEM402 3.0 20.6 1.0 C1A A:HEM402 3.0 20.0 1.0 C4A A:HEM402 3.0 20.1 1.0 C1B A:HEM402 3.1 19.3 1.0 C4B A:HEM402 3.1 19.7 1.0 C1C A:HEM402 3.1 20.5 1.0 CHD A:HEM402 3.3 20.2 1.0 CHA A:HEM402 3.4 19.4 1.0 CHB A:HEM402 3.4 19.7 1.0 CB A:CYS330 3.5 24.3 1.0 CHC A:HEM402 3.5 20.3 1.0 O A:GLY220 4.1 31.1 1.0 C2D A:HEM402 4.2 19.9 1.0 C3A A:HEM402 4.2 20.7 1.0 CA A:CYS330 4.2 26.2 1.0 C2A A:HEM402 4.2 21.6 1.0 C3D A:HEM402 4.2 20.4 1.0 C3C A:HEM402 4.2 20.4 1.0 C2C A:HEM402 4.3 21.6 1.0 C2B A:HEM402 4.3 19.6 1.0 C3B A:HEM402 4.4 19.8 1.0 N A:GLY332 4.6 21.6 1.0 CAM A:EMZ401 4.7 37.5 1.0 C A:GLY220 4.8 30.4 1.0 C A:CYS330 4.8 26.4 1.0 N A:LEU331 4.9 22.8 1.0 CA A:GLY332 4.9 20.3 1.0

Iron binding site 2 out of 2 in the The Structure of A Carbohydrate Active P450


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of The Structure of A Carbohydrate Active P450 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe403 b:24.7 occ:1.00 FE B:HEM403 0.0 24.7 1.0 ND B:HEM403 1.9 22.4 1.0 NA B:HEM403 2.0 23.9 1.0 NC B:HEM403 2.1 23.5 1.0 NB B:HEM403 2.1 23.1 1.0 SG B:CYS330 2.4 22.1 1.0 C1D B:HEM403 2.9 23.1 1.0 C4D B:HEM403 2.9 22.3 1.0 C1A B:HEM403 3.0 23.3 1.0 C4C B:HEM403 3.0 25.6 1.0 C4A B:HEM403 3.1 22.4 1.0 C4B B:HEM403 3.1 21.6 1.0 C1B B:HEM403 3.1 21.4 1.0 C1C B:HEM403 3.2 21.7 1.0 CHD B:HEM403 3.4 25.7 1.0 CHA B:HEM403 3.4 22.3 1.0 CB B:CYS330 3.5 22.6 1.0 CHB B:HEM403 3.5 22.7 1.0 CHC B:HEM403 3.5 21.4 1.0 CA B:CYS330 4.1 21.9 1.0 C2D B:HEM403 4.1 23.3 1.0 C3D B:HEM403 4.2 24.0 1.0 C2A B:HEM403 4.2 23.4 1.0 O B:GLY220 4.2 29.9 1.0 C3A B:HEM403 4.3 22.4 1.0 CAM B:EMZ402 4.3 32.1 1.0 C3C B:HEM403 4.3 23.5 1.0 C2B B:HEM403 4.3 21.7 1.0 C2C B:HEM403 4.3 21.3 1.0 C3B B:HEM403 4.4 22.5 1.0 N B:GLY332 4.6 25.7 1.0 C B:CYS330 4.8 21.1 1.0 N B:LEU331 4.9 22.2 1.0 C B:GLY220 4.9 31.9 1.0 CA B:GLY332 4.9 25.6 1.0

C.S.Robb, L.Reisky, U.T.Bornscheuer, J.H.Hehemann. Specificity and Mechanism of Carbohydrate Demethylation By Cytochrome P450 Monooxygenases. Biochem. J. V. 475 3875 2018.
ISSN: ESSN 1470-8728
PubMed: 30404923
DOI: 10.1042/BCJ20180762