Iron in PDB 6k58: Structure of the CYP102A1 Haem Domain with N-Enanthyl-L-Prolyl-L- Phenylalanine

All present enzymatic activity of Structure of the CYP102A1 Haem Domain with N-Enanthyl-L-Prolyl-L- Phenylalanine:
1.14.14.1; 1.6.2.4;

The structure of Structure of the CYP102A1 Haem Domain with N-Enanthyl-L-Prolyl-L- Phenylalanine, PDB code: 6k58 was solved by J.K.Stanfield, C.Kasai, H.Sugimoto, Y.Shiro, Y.Watanabe, O.Shoji, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.32 / 1.41
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	59.055, 126.769, 149.000, 90.00, 90.00, 90.00
R / Rfree (%)	14.5 / 17.8

The binding sites of Iron atom in the Structure of the CYP102A1 Haem Domain with N-Enanthyl-L-Prolyl-L- Phenylalanine (pdb code 6k58). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Structure of the CYP102A1 Haem Domain with N-Enanthyl-L-Prolyl-L- Phenylalanine, PDB code: 6k58:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Structure of the CYP102A1 Haem Domain with N-Enanthyl-L-Prolyl-L- Phenylalanine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of the CYP102A1 Haem Domain with N-Enanthyl-L-Prolyl-L- Phenylalanine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:13.8 occ:0.50 FE A:HEM501 0.0 13.8 0.5 FE A:HEM501 0.1 14.5 0.5 ND A:HEM501 1.9 13.6 0.5 ND A:HEM501 2.0 13.2 0.5 NA A:HEM501 2.0 12.7 0.5 NA A:HEM501 2.0 12.7 0.5 NC A:HEM501 2.0 12.0 0.5 NB A:HEM501 2.1 13.3 0.5 NC A:HEM501 2.1 13.7 0.5 NB A:HEM501 2.1 13.5 0.5 SG A:CYS400 2.3 15.1 1.0 S A:DMS502 2.4 22.7 0.5 C1D A:HEM501 3.0 12.8 0.5 C1D A:HEM501 3.0 13.4 0.5 C4D A:HEM501 3.0 12.6 0.5 C4D A:HEM501 3.0 12.9 0.5 C4C A:HEM501 3.0 12.7 0.5 C4B A:HEM501 3.0 13.5 0.5 C4B A:HEM501 3.0 14.2 0.5 C4C A:HEM501 3.0 14.2 0.5 C1A A:HEM501 3.0 12.6 0.5 C1A A:HEM501 3.1 12.5 0.5 C1B A:HEM501 3.1 13.8 0.5 C1B A:HEM501 3.1 14.6 0.5 C1C A:HEM501 3.1 12.7 0.5 C4A A:HEM501 3.1 13.2 0.5 C1C A:HEM501 3.1 13.7 0.5 C4A A:HEM501 3.1 13.4 0.5 O A:DMS502 3.3 29.2 0.5 CB A:CYS400 3.3 13.6 1.0 CHD A:HEM501 3.4 13.0 0.5 CHD A:HEM501 3.4 14.1 0.5 CHA A:HEM501 3.4 13.2 0.5 CHA A:HEM501 3.4 13.4 0.5 CHC A:HEM501 3.4 14.1 0.5 CHC A:HEM501 3.4 13.5 0.5 CHB A:HEM501 3.5 13.2 0.5 CHB A:HEM501 3.5 13.6 0.5 C1 A:DMS502 3.7 26.6 0.5 C2 A:DMS502 3.7 18.4 0.5 CA A:CYS400 4.0 13.7 1.0 O A:ALA264 4.1 20.1 0.5 C3C A:HEM501 4.2 14.2 0.5 C2D A:HEM501 4.2 12.8 0.5 C2C A:HEM501 4.2 12.7 0.5 C3D A:HEM501 4.3 13.0 0.5 C3C A:HEM501 4.3 13.8 0.5 C2D A:HEM501 4.3 13.2 0.5 C2C A:HEM501 4.3 14.2 0.5 C2A A:HEM501 4.3 13.1 0.5 C3D A:HEM501 4.3 14.1 0.5 C2A A:HEM501 4.3 12.9 0.5 C3A A:HEM501 4.3 12.6 0.5 C3A A:HEM501 4.3 13.1 0.5 C2B A:HEM501 4.3 14.6 0.5 C2B A:HEM501 4.3 14.6 0.5 C3B A:HEM501 4.3 14.0 0.5 C3B A:HEM501 4.3 15.2 0.5 N A:GLY402 4.7 14.0 1.0 C A:ALA264 4.8 22.4 0.5 CB A:ALA264 4.8 23.3 0.5 C A:CYS400 4.8 13.7 1.0 N A:ILE401 4.9 12.8 1.0

Iron binding site 2 out of 4 in the Structure of the CYP102A1 Haem Domain with N-Enanthyl-L-Prolyl-L- Phenylalanine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of the CYP102A1 Haem Domain with N-Enanthyl-L-Prolyl-L- Phenylalanine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:14.5 occ:0.50 FE A:HEM501 0.0 14.5 0.5 FE A:HEM501 0.1 13.8 0.5 ND A:HEM501 1.9 13.6 0.5 ND A:HEM501 2.0 13.2 0.5 NA A:HEM501 2.0 12.7 0.5 NA A:HEM501 2.0 12.7 0.5 NC A:HEM501 2.0 13.7 0.5 NB A:HEM501 2.1 13.5 0.5 NC A:HEM501 2.1 12.0 0.5 NB A:HEM501 2.1 13.3 0.5 SG A:CYS400 2.3 15.1 1.0 S A:DMS502 2.4 22.7 0.5 C1D A:HEM501 2.9 13.4 0.5 C4D A:HEM501 3.0 12.6 0.5 C1D A:HEM501 3.0 12.8 0.5 C4D A:HEM501 3.0 12.9 0.5 C4C A:HEM501 3.0 14.2 0.5 C4B A:HEM501 3.0 14.2 0.5 C4C A:HEM501 3.0 12.7 0.5 C4B A:HEM501 3.0 13.5 0.5 C1B A:HEM501 3.0 14.6 0.5 C1A A:HEM501 3.0 12.5 0.5 C1A A:HEM501 3.1 12.6 0.5 C1C A:HEM501 3.1 13.7 0.5 C1C A:HEM501 3.1 12.7 0.5 C1B A:HEM501 3.1 13.8 0.5 C4A A:HEM501 3.1 13.4 0.5 C4A A:HEM501 3.1 13.2 0.5 O A:DMS502 3.2 29.2 0.5 CB A:CYS400 3.4 13.6 1.0 CHD A:HEM501 3.4 14.1 0.5 CHD A:HEM501 3.4 13.0 0.5 CHA A:HEM501 3.4 13.2 0.5 CHC A:HEM501 3.4 14.1 0.5 CHC A:HEM501 3.4 13.5 0.5 CHA A:HEM501 3.4 13.4 0.5 CHB A:HEM501 3.5 13.6 0.5 CHB A:HEM501 3.5 13.2 0.5 C1 A:DMS502 3.6 26.6 0.5 C2 A:DMS502 3.7 18.4 0.5 CA A:CYS400 4.0 13.7 1.0 O A:ALA264 4.0 20.1 0.5 C2D A:HEM501 4.2 12.8 0.5 C3C A:HEM501 4.2 13.8 0.5 C3C A:HEM501 4.2 14.2 0.5 C3D A:HEM501 4.2 13.0 0.5 C2C A:HEM501 4.2 14.2 0.5 C2A A:HEM501 4.3 13.1 0.5 C2C A:HEM501 4.3 12.7 0.5 C3A A:HEM501 4.3 13.1 0.5 C2B A:HEM501 4.3 14.6 0.5 C2D A:HEM501 4.3 13.2 0.5 C3B A:HEM501 4.3 15.2 0.5 C3D A:HEM501 4.3 14.1 0.5 C2A A:HEM501 4.3 12.9 0.5 C3A A:HEM501 4.3 12.6 0.5 C3B A:HEM501 4.3 14.0 0.5 C2B A:HEM501 4.3 14.6 0.5 C A:ALA264 4.7 22.4 0.5 CB A:ALA264 4.7 23.3 0.5 N A:GLY402 4.8 14.0 1.0 C A:CYS400 4.8 13.7 1.0 N A:ILE401 4.9 12.8 1.0 CB A:ALA264 5.0 16.3 0.5

Iron binding site 3 out of 4 in the Structure of the CYP102A1 Haem Domain with N-Enanthyl-L-Prolyl-L- Phenylalanine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structure of the CYP102A1 Haem Domain with N-Enanthyl-L-Prolyl-L- Phenylalanine within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:15.3 occ:0.45 FE B:HEM501 0.0 15.3 0.5 FE B:HEM501 0.0 15.1 0.6 ND B:HEM501 1.9 13.9 0.5 ND B:HEM501 2.0 15.4 0.6 NA B:HEM501 2.0 13.8 0.6 NA B:HEM501 2.0 15.6 0.5 NC B:HEM501 2.1 13.8 0.6 NC B:HEM501 2.1 15.0 0.5 NB B:HEM501 2.1 14.8 0.5 NB B:HEM501 2.1 14.9 0.6 SG B:CYS400 2.3 16.4 1.0 S B:DMS502 2.4 24.2 0.5 C1D B:HEM501 2.9 13.6 0.5 C4D B:HEM501 3.0 14.2 0.5 C1D B:HEM501 3.0 14.4 0.6 C4D B:HEM501 3.0 14.5 0.6 C4B B:HEM501 3.0 14.6 0.5 C4B B:HEM501 3.0 15.3 0.6 C4C B:HEM501 3.0 14.9 0.5 C4C B:HEM501 3.0 14.6 0.6 C1B B:HEM501 3.0 15.7 0.6 C1A B:HEM501 3.1 14.7 0.5 C1A B:HEM501 3.1 14.1 0.6 C1C B:HEM501 3.1 14.1 0.6 C4A B:HEM501 3.1 13.7 0.6 C1B B:HEM501 3.1 14.5 0.5 C1C B:HEM501 3.1 15.1 0.5 C4A B:HEM501 3.1 14.3 0.5 O B:DMS502 3.1 35.7 0.5 CB B:CYS400 3.4 14.9 1.0 CHD B:HEM501 3.4 14.3 0.5 CHD B:HEM501 3.4 15.2 0.6 CHC B:HEM501 3.4 15.0 0.6 CHC B:HEM501 3.4 15.1 0.5 CHA B:HEM501 3.4 15.5 0.5 CHA B:HEM501 3.4 14.5 0.6 CHB B:HEM501 3.4 14.6 0.6 CHB B:HEM501 3.5 15.5 0.5 C2 B:DMS502 3.6 20.9 0.5 C1 B:DMS502 3.6 31.2 0.5 CA B:CYS400 4.0 15.1 1.0 O B:ALA264 4.1 21.5 0.5 C2D B:HEM501 4.2 14.5 0.5 C3C B:HEM501 4.2 14.6 0.5 C3D B:HEM501 4.2 15.4 0.5 C2C B:HEM501 4.2 14.4 0.5 C3C B:HEM501 4.2 15.8 0.6 C2C B:HEM501 4.2 14.5 0.6 C3A B:HEM501 4.3 14.2 0.6 C2A B:HEM501 4.3 15.0 0.6 C2B B:HEM501 4.3 16.5 0.6 C2D B:HEM501 4.3 14.7 0.6 C2B B:HEM501 4.3 15.2 0.5 C2A B:HEM501 4.3 14.3 0.5 C3B B:HEM501 4.3 15.3 0.5 C3A B:HEM501 4.3 14.0 0.5 C3D B:HEM501 4.3 14.3 0.6 C3B B:HEM501 4.3 16.1 0.6 CB B:ALA264 4.7 20.7 0.5 C B:ALA264 4.7 21.6 0.5 N B:GLY402 4.8 14.9 1.0 C B:CYS400 4.8 15.2 1.0 N B:ILE401 4.9 14.2 1.0

Iron binding site 4 out of 4 in the Structure of the CYP102A1 Haem Domain with N-Enanthyl-L-Prolyl-L- Phenylalanine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structure of the CYP102A1 Haem Domain with N-Enanthyl-L-Prolyl-L- Phenylalanine within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:15.1 occ:0.55 FE B:HEM501 0.0 15.1 0.6 FE B:HEM501 0.0 15.3 0.5 ND B:HEM501 1.9 15.4 0.6 ND B:HEM501 1.9 13.9 0.5 NA B:HEM501 2.0 15.6 0.5 NC B:HEM501 2.0 13.8 0.6 NA B:HEM501 2.0 13.8 0.6 NB B:HEM501 2.0 14.8 0.5 NC B:HEM501 2.1 15.0 0.5 NB B:HEM501 2.1 14.9 0.6 SG B:CYS400 2.3 16.4 1.0 S B:DMS502 2.4 24.2 0.5 C1D B:HEM501 3.0 13.6 0.5 C1D B:HEM501 3.0 14.4 0.6 C4D B:HEM501 3.0 14.2 0.5 C4D B:HEM501 3.0 14.5 0.6 C4B B:HEM501 3.0 14.6 0.5 C4C B:HEM501 3.0 14.6 0.6 C4B B:HEM501 3.0 15.3 0.6 C1B B:HEM501 3.0 14.5 0.5 C4C B:HEM501 3.0 14.9 0.5 C1C B:HEM501 3.0 14.1 0.6 C1A B:HEM501 3.1 14.7 0.5 C1C B:HEM501 3.1 15.1 0.5 C1B B:HEM501 3.1 15.7 0.6 C1A B:HEM501 3.1 14.1 0.6 C4A B:HEM501 3.1 14.3 0.5 C4A B:HEM501 3.1 13.7 0.6 O B:DMS502 3.2 35.7 0.5 CB B:CYS400 3.3 14.9 1.0 CHD B:HEM501 3.4 15.2 0.6 CHC B:HEM501 3.4 15.0 0.6 CHD B:HEM501 3.4 14.3 0.5 CHC B:HEM501 3.4 15.1 0.5 CHA B:HEM501 3.4 15.5 0.5 CHA B:HEM501 3.5 14.5 0.6 CHB B:HEM501 3.5 15.5 0.5 CHB B:HEM501 3.5 14.6 0.6 C2 B:DMS502 3.7 20.9 0.5 C1 B:DMS502 3.7 31.2 0.5 CA B:CYS400 4.0 15.1 1.0 O B:ALA264 4.1 21.5 0.5 C3C B:HEM501 4.2 15.8 0.6 C2C B:HEM501 4.2 14.5 0.6 C2D B:HEM501 4.2 14.5 0.5 C2C B:HEM501 4.2 14.4 0.5 C3C B:HEM501 4.2 14.6 0.5 C3D B:HEM501 4.3 15.4 0.5 C2B B:HEM501 4.3 15.2 0.5 C2D B:HEM501 4.3 14.7 0.6 C3B B:HEM501 4.3 15.3 0.5 C3A B:HEM501 4.3 14.0 0.5 C2A B:HEM501 4.3 14.3 0.5 C3D B:HEM501 4.3 14.3 0.6 C2B B:HEM501 4.3 16.5 0.6 C2A B:HEM501 4.3 15.0 0.6 C3A B:HEM501 4.3 14.2 0.6 C3B B:HEM501 4.3 16.1 0.6 CB B:ALA264 4.7 20.7 0.5 N B:GLY402 4.8 14.9 1.0 C B:ALA264 4.8 21.6 0.5 C B:CYS400 4.8 15.2 1.0 N B:ILE401 4.9 14.2 1.0

O.Shoji, J.K.Stanfield. Structure of CYP102A1 Haem Domain with N-Enanthyl-L-Prolyl-L-Phenylalanine at 1.41 Angstrom Resolution To Be Published.