Iron in PDB 6js8: Structure of the CYP102A1 Haem Domain with N-Dehydroabietoyl-L- Tryptophan

All present enzymatic activity of Structure of the CYP102A1 Haem Domain with N-Dehydroabietoyl-L- Tryptophan:
1.14.14.1; 1.6.2.4;

The structure of Structure of the CYP102A1 Haem Domain with N-Dehydroabietoyl-L- Tryptophan, PDB code: 6js8 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)	47.91 / 1.36
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	58.886, 148.789, 63.196, 90.00, 98.42, 90.00
R / Rfree (%)	13.2 / 15.9

The binding sites of Iron atom in the Structure of the CYP102A1 Haem Domain with N-Dehydroabietoyl-L- Tryptophan (pdb code 6js8). 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-Dehydroabietoyl-L- Tryptophan, PDB code: 6js8:
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-Dehydroabietoyl-L- Tryptophan


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-Dehydroabietoyl-L- Tryptophan within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:13.4 occ:0.50 FE A:HEM501 0.0 13.4 0.5 FE A:HEM501 0.0 13.2 0.5 ND A:HEM501 1.9 12.9 0.5 ND A:HEM501 2.0 13.0 0.5 NA A:HEM501 2.0 12.8 0.5 NA A:HEM501 2.0 12.9 0.5 NB A:HEM501 2.0 12.8 0.5 NC A:HEM501 2.1 12.8 0.5 NC A:HEM501 2.1 12.4 0.5 NB A:HEM501 2.1 13.4 0.5 SG A:CYS400 2.3 14.3 1.0 S A:DMS502 2.4 16.8 0.6 C1D A:HEM501 2.9 13.0 0.5 C4D A:HEM501 3.0 12.5 0.5 C1D A:HEM501 3.0 12.6 0.5 C4D A:HEM501 3.0 12.7 0.5 C4B A:HEM501 3.0 13.1 0.5 C4C A:HEM501 3.0 12.6 0.5 C4C A:HEM501 3.0 13.1 0.5 C1B A:HEM501 3.0 12.0 0.5 C4B A:HEM501 3.0 13.7 0.5 C1A A:HEM501 3.0 12.3 0.5 C1B A:HEM501 3.0 13.8 0.5 C4A A:HEM501 3.0 13.3 0.5 C1A A:HEM501 3.1 12.8 0.5 C4A A:HEM501 3.1 12.5 0.5 C1C A:HEM501 3.1 13.5 0.5 C1C A:HEM501 3.1 12.8 0.5 CB A:CYS400 3.3 13.1 1.0 CHD A:HEM501 3.4 12.6 0.5 O A:DMS502 3.4 22.6 0.6 CHD A:HEM501 3.4 12.7 0.5 CHA A:HEM501 3.4 12.6 0.5 CHA A:HEM501 3.4 12.2 0.5 CHB A:HEM501 3.4 12.5 0.5 CHC A:HEM501 3.4 13.3 0.5 CHB A:HEM501 3.5 13.1 0.5 CHC A:HEM501 3.5 14.2 0.5 C1 A:DMS502 3.5 18.4 0.6 C2 A:DMS502 3.6 17.1 0.6 CA A:CYS400 4.0 12.1 1.0 C2D A:HEM501 4.2 12.6 0.5 C3D A:HEM501 4.2 12.8 0.5 C3C A:HEM501 4.2 13.8 0.5 C3A A:HEM501 4.2 13.7 0.5 C2A A:HEM501 4.2 12.7 0.5 C2B A:HEM501 4.3 12.8 0.5 C3C A:HEM501 4.3 13.6 0.5 C3B A:HEM501 4.3 14.1 0.5 C2C A:HEM501 4.3 14.2 0.5 C2D A:HEM501 4.3 12.6 0.5 C2B A:HEM501 4.3 13.9 0.5 C2C A:HEM501 4.3 13.7 0.5 C3D A:HEM501 4.3 12.6 0.5 C3A A:HEM501 4.3 12.5 0.5 C2A A:HEM501 4.3 12.5 0.5 C3B A:HEM501 4.3 14.7 0.5 N A:GLY402 4.8 13.1 1.0 C A:CYS400 4.8 12.7 1.0 CB A:ALA264 4.9 22.1 1.0 N A:ILE401 4.9 12.6 1.0

Iron binding site 2 out of 4 in the Structure of the CYP102A1 Haem Domain with N-Dehydroabietoyl-L- Tryptophan


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-Dehydroabietoyl-L- Tryptophan within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:13.2 occ:0.50 FE A:HEM501 0.0 13.2 0.5 FE A:HEM501 0.0 13.4 0.5 ND A:HEM501 1.9 12.9 0.5 ND A:HEM501 1.9 13.0 0.5 NA A:HEM501 2.0 12.9 0.5 NA A:HEM501 2.0 12.8 0.5 NC A:HEM501 2.1 12.4 0.5 NB A:HEM501 2.1 13.4 0.5 NB A:HEM501 2.1 12.8 0.5 NC A:HEM501 2.1 12.8 0.5 SG A:CYS400 2.3 14.3 1.0 S A:DMS502 2.4 16.8 0.6 C1D A:HEM501 2.9 12.6 0.5 C1D A:HEM501 3.0 13.0 0.5 C4D A:HEM501 3.0 12.7 0.5 C4D A:HEM501 3.0 12.5 0.5 C4C A:HEM501 3.0 13.1 0.5 C1B A:HEM501 3.0 13.8 0.5 C4B A:HEM501 3.0 13.1 0.5 C4B A:HEM501 3.0 13.7 0.5 C1A A:HEM501 3.0 12.8 0.5 C1A A:HEM501 3.1 12.3 0.5 C4A A:HEM501 3.1 12.5 0.5 C4C A:HEM501 3.1 12.6 0.5 C1B A:HEM501 3.1 12.0 0.5 C4A A:HEM501 3.1 13.3 0.5 C1C A:HEM501 3.1 12.8 0.5 C1C A:HEM501 3.1 13.5 0.5 CB A:CYS400 3.3 13.1 1.0 CHD A:HEM501 3.4 12.7 0.5 O A:DMS502 3.4 22.6 0.6 CHD A:HEM501 3.4 12.6 0.5 CHA A:HEM501 3.4 12.6 0.5 CHA A:HEM501 3.4 12.2 0.5 CHB A:HEM501 3.4 13.1 0.5 CHC A:HEM501 3.5 13.3 0.5 CHC A:HEM501 3.5 14.2 0.5 CHB A:HEM501 3.5 12.5 0.5 C1 A:DMS502 3.5 18.4 0.6 C2 A:DMS502 3.6 17.1 0.6 CA A:CYS400 4.0 12.1 1.0 C3C A:HEM501 4.2 13.6 0.5 C2D A:HEM501 4.2 12.6 0.5 C2D A:HEM501 4.2 12.6 0.5 C2B A:HEM501 4.3 13.9 0.5 C3D A:HEM501 4.3 12.8 0.5 C2C A:HEM501 4.3 13.7 0.5 C3A A:HEM501 4.3 12.5 0.5 C3D A:HEM501 4.3 12.6 0.5 C2A A:HEM501 4.3 12.7 0.5 C3A A:HEM501 4.3 13.7 0.5 C3C A:HEM501 4.3 13.8 0.5 C2A A:HEM501 4.3 12.5 0.5 C2B A:HEM501 4.3 12.8 0.5 C3B A:HEM501 4.3 14.1 0.5 C3B A:HEM501 4.3 14.7 0.5 C2C A:HEM501 4.3 14.2 0.5 C A:CYS400 4.8 12.7 1.0 N A:GLY402 4.8 13.1 1.0 N A:ILE401 4.9 12.6 1.0 CB A:ALA264 4.9 22.1 1.0

Iron binding site 3 out of 4 in the Structure of the CYP102A1 Haem Domain with N-Dehydroabietoyl-L- Tryptophan


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-Dehydroabietoyl-L- Tryptophan within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:13.8 occ:0.50 FE B:HEM501 0.0 13.8 0.5 FE B:HEM501 0.0 14.0 0.5 ND B:HEM501 1.9 12.7 0.5 ND B:HEM501 2.0 13.5 0.5 NA B:HEM501 2.0 13.0 0.5 NA B:HEM501 2.0 13.2 0.5 NB B:HEM501 2.0 13.4 0.5 NC B:HEM501 2.1 13.2 0.5 NC B:HEM501 2.1 12.2 0.5 NB B:HEM501 2.1 13.0 0.5 SG B:CYS400 2.3 14.8 1.0 S B:DMS502 2.4 18.7 0.6 C1D B:HEM501 2.9 12.9 0.5 C1D B:HEM501 3.0 13.4 0.5 C4D B:HEM501 3.0 13.2 0.5 C4D B:HEM501 3.0 13.1 0.5 C4B B:HEM501 3.0 13.3 0.5 C4C B:HEM501 3.0 13.2 0.5 C4B B:HEM501 3.0 13.7 0.5 C1B B:HEM501 3.0 13.6 0.5 C4C B:HEM501 3.0 13.0 0.5 C1A B:HEM501 3.0 13.5 0.5 C4A B:HEM501 3.0 13.9 0.5 C1A B:HEM501 3.1 12.9 0.5 C1B B:HEM501 3.1 13.0 0.5 C1C B:HEM501 3.1 13.3 0.5 C4A B:HEM501 3.1 13.2 0.5 C1C B:HEM501 3.1 13.2 0.5 CB B:CYS400 3.4 13.9 1.0 CHD B:HEM501 3.4 13.0 0.5 O B:DMS502 3.4 21.7 0.6 CHD B:HEM501 3.4 13.3 0.5 CHA B:HEM501 3.4 13.2 0.5 CHA B:HEM501 3.4 13.4 0.5 CHB B:HEM501 3.4 13.6 0.5 CHC B:HEM501 3.4 13.6 0.5 CHC B:HEM501 3.4 13.7 0.5 CHB B:HEM501 3.5 13.2 0.5 C2 B:DMS502 3.5 20.7 0.6 C1 B:DMS502 3.5 17.1 0.6 CA B:CYS400 4.0 13.6 1.0 C2D B:HEM501 4.2 12.6 0.5 C3A B:HEM501 4.2 14.6 0.5 C3C B:HEM501 4.2 14.0 0.5 C3C B:HEM501 4.2 14.2 0.5 C3D B:HEM501 4.3 12.8 0.5 C2A B:HEM501 4.3 13.3 0.5 C2D B:HEM501 4.3 13.9 0.5 C2B B:HEM501 4.3 14.1 0.5 C2C B:HEM501 4.3 14.4 0.5 C2C B:HEM501 4.3 14.0 0.5 C3B B:HEM501 4.3 14.4 0.5 C3D B:HEM501 4.3 13.8 0.5 C2B B:HEM501 4.3 14.0 0.5 C3A B:HEM501 4.3 13.6 0.5 C2A B:HEM501 4.3 13.5 0.5 C3B B:HEM501 4.3 14.4 0.5 C B:CYS400 4.8 13.5 1.0 N B:GLY402 4.8 13.6 1.0 CB B:ALA264 4.9 26.5 1.0 N B:ILE401 4.9 14.1 1.0

Iron binding site 4 out of 4 in the Structure of the CYP102A1 Haem Domain with N-Dehydroabietoyl-L- Tryptophan


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-Dehydroabietoyl-L- Tryptophan within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:14.0 occ:0.50 FE B:HEM501 0.0 14.0 0.5 FE B:HEM501 0.0 13.8 0.5 ND B:HEM501 1.9 13.5 0.5 ND B:HEM501 1.9 12.7 0.5 NA B:HEM501 2.0 13.2 0.5 NA B:HEM501 2.0 13.0 0.5 NC B:HEM501 2.1 12.2 0.5 NB B:HEM501 2.1 13.0 0.5 NB B:HEM501 2.1 13.4 0.5 NC B:HEM501 2.1 13.2 0.5 SG B:CYS400 2.3 14.8 1.0 S B:DMS502 2.4 18.7 0.6 C1D B:HEM501 2.9 13.4 0.5 C1D B:HEM501 3.0 12.9 0.5 C4D B:HEM501 3.0 13.1 0.5 C4D B:HEM501 3.0 13.2 0.5 C4C B:HEM501 3.0 13.0 0.5 C4B B:HEM501 3.0 13.7 0.5 C4B B:HEM501 3.0 13.3 0.5 C1B B:HEM501 3.0 13.0 0.5 C1A B:HEM501 3.0 12.9 0.5 C4A B:HEM501 3.1 13.2 0.5 C1A B:HEM501 3.1 13.5 0.5 C4C B:HEM501 3.1 13.2 0.5 C1B B:HEM501 3.1 13.6 0.5 C1C B:HEM501 3.1 13.3 0.5 C4A B:HEM501 3.1 13.9 0.5 C1C B:HEM501 3.1 13.2 0.5 CB B:CYS400 3.3 13.9 1.0 CHD B:HEM501 3.4 13.3 0.5 O B:DMS502 3.4 21.7 0.6 CHD B:HEM501 3.4 13.0 0.5 CHA B:HEM501 3.4 13.2 0.5 CHA B:HEM501 3.4 13.4 0.5 CHB B:HEM501 3.4 13.2 0.5 CHC B:HEM501 3.4 13.6 0.5 CHC B:HEM501 3.4 13.7 0.5 CHB B:HEM501 3.5 13.6 0.5 C1 B:DMS502 3.5 17.1 0.6 C2 B:DMS502 3.5 20.7 0.6 CA B:CYS400 4.0 13.6 1.0 C3C B:HEM501 4.2 14.2 0.5 C2D B:HEM501 4.2 13.9 0.5 C2C B:HEM501 4.2 14.4 0.5 C2D B:HEM501 4.3 12.6 0.5 C3A B:HEM501 4.3 13.6 0.5 C3D B:HEM501 4.3 13.8 0.5 C2B B:HEM501 4.3 14.0 0.5 C2A B:HEM501 4.3 13.5 0.5 C3D B:HEM501 4.3 12.8 0.5 C3A B:HEM501 4.3 14.6 0.5 C2A B:HEM501 4.3 13.3 0.5 C3C B:HEM501 4.3 14.0 0.5 C3B B:HEM501 4.3 14.4 0.5 C2B B:HEM501 4.3 14.1 0.5 C2C B:HEM501 4.3 14.0 0.5 C3B B:HEM501 4.3 14.4 0.5 C B:CYS400 4.8 13.5 1.0 N B:GLY402 4.8 13.6 1.0 CB B:ALA264 4.9 26.5 1.0 N B:ILE401 4.9 14.1 1.0

O.Shoji, J.K.Stanfield. Structure of CYP102A1 Haem Domain with N-Dehydroabietoyl-L-Tryptophan at 1.36 Angstrom Resolution To Be Published.