Iron in PDB 6w0s: Crystal Structure of Substrate Free Cytochrome P450 NASF5053 From Streptomyces Sp. Nrrl F-5053

The structure of Crystal Structure of Substrate Free Cytochrome P450 NASF5053 From Streptomyces Sp. Nrrl F-5053, PDB code: 6w0s was solved by Z.Luo, X.Jia, C.Sun, X.Qu, B.Kobe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.06 / 1.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.208, 91.325, 98.275, 90.00, 96.41, 90.00
R / Rfree (%)	18.6 / 22

The structure of Crystal Structure of Substrate Free Cytochrome P450 NASF5053 From Streptomyces Sp. Nrrl F-5053 also contains other interesting chemical elements:

Bromine	(Br)	4 atoms
Chlorine	(Cl)	6 atoms
Sodium	(Na)	2 atoms

The binding sites of Iron atom in the Crystal Structure of Substrate Free Cytochrome P450 NASF5053 From Streptomyces Sp. Nrrl F-5053 (pdb code 6w0s). 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 Substrate Free Cytochrome P450 NASF5053 From Streptomyces Sp. Nrrl F-5053, PDB code: 6w0s:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Substrate Free Cytochrome P450 NASF5053 From Streptomyces Sp. Nrrl F-5053


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 Substrate Free Cytochrome P450 NASF5053 From Streptomyces Sp. Nrrl F-5053 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe409 b:12.8 occ:1.00 FE A:HEM409 0.0 12.8 1.0 NA A:HEM409 2.0 11.0 1.0 NB A:HEM409 2.0 11.5 1.0 ND A:HEM409 2.0 12.2 1.0 NC A:HEM409 2.0 9.3 1.0 O A:HOH525 2.3 19.0 1.0 SG A:CYS348 2.3 13.2 1.0 C4C A:HEM409 3.0 15.6 1.0 C1A A:HEM409 3.0 11.1 1.0 C4A A:HEM409 3.0 14.0 1.0 C4B A:HEM409 3.0 10.5 1.0 C1C A:HEM409 3.0 10.0 1.0 C1D A:HEM409 3.1 12.4 1.0 C1B A:HEM409 3.1 14.7 1.0 C4D A:HEM409 3.1 11.4 1.0 HB2 A:CYS348 3.1 10.3 1.0 CB A:CYS348 3.4 8.6 1.0 CHD A:HEM409 3.4 14.5 1.0 CHA A:HEM409 3.4 12.3 1.0 CHC A:HEM409 3.4 14.1 1.0 CHB A:HEM409 3.4 16.3 1.0 H A:GLY350 3.9 14.3 1.0 HA A:CYS348 3.9 13.9 1.0 HD2 A:PRO349 4.0 16.1 1.0 HB1 A:ALA237 4.1 21.8 1.0 HB3 A:CYS348 4.1 10.3 1.0 O A:ALA237 4.2 17.0 1.0 C3C A:HEM409 4.2 10.8 1.0 CA A:CYS348 4.2 11.6 1.0 C3A A:HEM409 4.2 12.4 1.0 C2A A:HEM409 4.2 13.9 1.0 C2C A:HEM409 4.2 12.8 1.0 C2B A:HEM409 4.3 10.3 1.0 C3B A:HEM409 4.3 14.1 1.0 C2D A:HEM409 4.3 14.2 1.0 HO3 A:GOL401 4.3 42.7 1.0 HA3 A:GLY350 4.3 15.2 1.0 C3D A:HEM409 4.3 13.8 1.0 O3 A:GOL401 4.3 35.6 1.0 HHA A:HEM409 4.4 14.7 1.0 HHC A:HEM409 4.4 16.9 1.0 HHB A:HEM409 4.4 19.5 1.0 HG21 A:THR241 4.5 18.3 1.0 H31 A:GOL401 4.6 33.5 1.0 HD1 A:PHE341 4.6 15.7 1.0 N A:GLY350 4.7 11.9 1.0 HG1 A:THR241 4.7 17.7 1.0 C A:CYS348 4.9 14.8 1.0 CD A:PRO349 4.9 13.5 1.0 CA A:GLY350 4.9 12.7 1.0 C3 A:GOL401 5.0 27.9 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Substrate Free Cytochrome P450 NASF5053 From Streptomyces Sp. Nrrl F-5053


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 Substrate Free Cytochrome P450 NASF5053 From Streptomyces Sp. Nrrl F-5053 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe406 b:12.2 occ:1.00 FE B:HEM406 0.0 12.2 1.0 NB B:HEM406 2.0 10.4 1.0 NA B:HEM406 2.0 8.4 1.0 NC B:HEM406 2.0 6.9 1.0 ND B:HEM406 2.0 13.0 1.0 O B:HOH593 2.3 19.2 1.0 SG B:CYS348 2.3 12.5 1.0 C4B B:HEM406 3.0 10.4 1.0 C1C B:HEM406 3.0 10.7 1.0 C1A B:HEM406 3.0 12.8 1.0 C4C B:HEM406 3.0 13.5 1.0 C4A B:HEM406 3.0 13.0 1.0 C1B B:HEM406 3.0 10.9 1.0 C4D B:HEM406 3.1 10.2 1.0 C1D B:HEM406 3.1 12.2 1.0 HB2 B:CYS348 3.2 9.5 1.0 CHC B:HEM406 3.4 11.9 1.0 CB B:CYS348 3.4 8.0 1.0 CHA B:HEM406 3.4 11.2 1.0 CHD B:HEM406 3.5 15.9 1.0 CHB B:HEM406 3.5 14.5 1.0 HA B:CYS348 3.9 14.3 1.0 H B:GLY350 3.9 13.3 1.0 HD2 B:PRO349 4.1 18.6 1.0 HB3 B:CYS348 4.2 9.5 1.0 O B:ALA237 4.2 16.3 1.0 HB1 B:ALA237 4.2 21.2 1.0 CA B:CYS348 4.2 12.0 1.0 C3C B:HEM406 4.2 10.8 1.0 C2C B:HEM406 4.2 9.5 1.0 C3B B:HEM406 4.2 14.4 1.0 C2B B:HEM406 4.2 12.3 1.0 C2A B:HEM406 4.2 15.3 1.0 C3A B:HEM406 4.2 13.7 1.0 C2D B:HEM406 4.3 14.5 1.0 C3D B:HEM406 4.3 13.5 1.0 HA3 B:GLY350 4.3 19.4 1.0 HHC B:HEM406 4.3 14.2 1.0 HHA B:HEM406 4.4 13.5 1.0 HHD B:HEM406 4.4 19.1 1.0 HHB B:HEM406 4.4 17.4 1.0 O B:HOH808 4.5 28.5 1.0 HD1 B:PHE341 4.6 15.6 1.0 N B:GLY350 4.7 11.1 1.0 C B:CYS348 4.9 12.6 1.0 CA B:GLY350 4.9 16.2 1.0 CD B:PRO349 5.0 15.5 1.0

C.Sun, Z.Luo, W.Zhang, Z.Deng, M.Mobli, B.Kobe, X.Jia, X.Qu. Molecular Basis of Regio- and Stereo-Specificity in Biosynthesis of Bacterial Heterodimeric Diketopiperazines To Be Published.