Iron in PDB 4c9m: Structure of Substrate Free, Glycerol Bound Wild Type CYP101D1

The structure of Structure of Substrate Free, Glycerol Bound Wild Type CYP101D1, PDB code: 4c9m was solved by D.Batabyal, T.L Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.076 / 1.80
Space group	P 64 2 2
Cell size a, b, c (Å), α, β, γ (°)	151.520, 151.520, 195.682, 90.00, 90.00, 120.00
R / Rfree (%)	15.42 / 18.8

The binding sites of Iron atom in the Structure of Substrate Free, Glycerol Bound Wild Type CYP101D1 (pdb code 4c9m). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of Substrate Free, Glycerol Bound Wild Type CYP101D1, PDB code: 4c9m:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of Substrate Free, Glycerol Bound Wild Type CYP101D1


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Substrate Free, Glycerol Bound Wild Type CYP101D1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1418 b:12.7 occ:1.00 FE A:HEM1418 0.0 12.7 1.0 NA A:HEM1418 2.0 10.7 1.0 ND A:HEM1418 2.0 12.9 1.0 NC A:HEM1418 2.0 11.3 1.0 NB A:HEM1418 2.0 12.4 1.0 SG A:CYS365 2.3 13.3 1.0 O A:HOH2383 2.4 15.7 1.0 C4D A:HEM1418 3.0 11.6 1.0 C1A A:HEM1418 3.0 11.3 1.0 C1D A:HEM1418 3.0 11.7 1.0 C1C A:HEM1418 3.0 12.2 1.0 C4A A:HEM1418 3.0 9.8 1.0 C4B A:HEM1418 3.1 11.2 1.0 C1B A:HEM1418 3.1 9.6 1.0 C4C A:HEM1418 3.1 11.8 1.0 HB2 A:CYS365 3.3 16.2 1.0 CHA A:HEM1418 3.4 12.7 1.0 CHC A:HEM1418 3.4 11.1 1.0 CHD A:HEM1418 3.4 12.5 1.0 CHB A:HEM1418 3.4 9.7 1.0 CB A:CYS365 3.4 13.5 1.0 HA A:CYS365 3.7 13.3 1.0 H A:GLY367 3.8 17.4 1.0 HO2 A:GOL1419 3.9 51.5 1.0 O2 A:GOL1419 4.0 42.9 1.0 CA A:CYS365 4.1 11.1 1.0 H11 A:GOL1419 4.2 50.1 1.0 HB3 A:CYS365 4.2 16.2 1.0 C2A A:HEM1418 4.3 11.9 1.0 C3D A:HEM1418 4.3 11.5 1.0 C3A A:HEM1418 4.3 10.7 1.0 C2C A:HEM1418 4.3 15.5 1.0 C3B A:HEM1418 4.3 11.7 1.0 C2D A:HEM1418 4.3 12.8 1.0 C3C A:HEM1418 4.3 14.5 1.0 HG22 A:THR260 4.3 24.2 0.4 C2B A:HEM1418 4.3 10.8 1.0 HHA A:HEM1418 4.4 15.2 1.0 HHD A:HEM1418 4.4 15.0 1.0 HA3 A:GLY367 4.4 19.4 1.0 HHB A:HEM1418 4.4 11.7 1.0 HHC A:HEM1418 4.4 13.3 1.0 H A:ALA366 4.5 15.8 1.0 N A:GLY367 4.6 14.5 1.0 HA3 A:GLY256 4.6 20.4 1.0 HD1 A:PHE358 4.6 13.6 1.0 HG22 A:THR260 4.7 21.3 0.6 O1 A:GOL1419 4.7 48.1 1.0 C A:CYS365 4.7 13.2 1.0 N A:ALA366 4.8 13.2 1.0 C1 A:GOL1419 4.8 41.8 1.0 CA A:GLY367 4.9 16.2 1.0 HO1 A:GOL1419 4.9 57.8 1.0 C2 A:GOL1419 5.0 45.5 1.0 HA2 A:GLY256 5.0 20.4 1.0

Iron binding site 2 out of 2 in the Structure of Substrate Free, Glycerol Bound Wild Type CYP101D1


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Substrate Free, Glycerol Bound Wild Type CYP101D1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe1418 b:11.9 occ:1.00 FE B:HEM1418 0.0 11.9 1.0 NB B:HEM1418 2.0 11.0 1.0 ND B:HEM1418 2.0 12.7 1.0 NA B:HEM1418 2.0 10.0 1.0 NC B:HEM1418 2.1 9.1 1.0 SG B:CYS365 2.3 14.3 1.0 O B:HOH2307 2.5 18.8 1.0 C1B B:HEM1418 3.0 11.5 1.0 C1C B:HEM1418 3.0 11.4 1.0 C4A B:HEM1418 3.0 12.4 1.0 C4B B:HEM1418 3.0 11.1 1.0 C1A B:HEM1418 3.1 12.3 1.0 C1D B:HEM1418 3.1 14.7 1.0 C4C B:HEM1418 3.1 13.4 1.0 C4D B:HEM1418 3.1 11.9 1.0 HB2 B:CYS365 3.2 13.9 1.0 CB B:CYS365 3.4 11.6 1.0 CHB B:HEM1418 3.4 12.8 1.0 CHC B:HEM1418 3.4 15.7 1.0 CHD B:HEM1418 3.5 12.6 1.0 CHA B:HEM1418 3.5 11.9 1.0 HA B:CYS365 3.7 14.7 1.0 H B:GLY367 3.7 17.7 1.0 CA B:CYS365 4.1 12.3 1.0 O2 B:GOL1419 4.1 41.5 1.0 HB3 B:CYS365 4.2 13.9 1.0 C2B B:HEM1418 4.2 11.5 1.0 C2C B:HEM1418 4.3 11.9 1.0 C3C B:HEM1418 4.3 11.5 1.0 C3A B:HEM1418 4.3 8.3 1.0 C3B B:HEM1418 4.3 11.1 1.0 C2A B:HEM1418 4.3 9.8 1.0 HG22 B:THR260 4.3 21.9 0.5 C2D B:HEM1418 4.3 14.1 1.0 HA3 B:GLY367 4.3 18.5 1.0 C3D B:HEM1418 4.3 12.8 1.0 HG1 B:THR260 4.4 27.4 0.6 HO2 B:GOL1419 4.4 49.8 1.0 H B:ALA366 4.4 15.1 1.0 HG1 B:THR260 4.5 26.9 0.5 H32 B:GOL1419 4.5 63.6 1.0 N B:GLY367 4.5 14.8 1.0 HD1 B:PHE358 4.6 15.6 1.0 HG22 B:THR260 4.6 14.6 0.6 HA3 B:GLY256 4.6 27.9 1.0 C B:CYS365 4.7 12.9 1.0 N B:ALA366 4.7 12.5 1.0 CA B:GLY367 4.8 15.4 1.0 HA2 B:GLY256 4.9 27.9 1.0

D.Batabyal, T.L.Poulos. Crystal Structures and Functional Characterization of Wild Type and Active Sites Mutants of CYP101D1. Biochemistry V. 52 8898 2013.
ISSN: ISSN 0006-2960
PubMed: 24261604
DOI: 10.1021/BI401330C