Rhodium in PDB 6k24: Structure of the Rhodium Mesoporphyrin IX-Reconstituted CYP102A1 Haem Domain with N-Abietoyl-L-Tryptophan

All present enzymatic activity of Structure of the Rhodium Mesoporphyrin IX-Reconstituted CYP102A1 Haem Domain with N-Abietoyl-L-Tryptophan:
1.14.14.1; 1.6.2.4;

The structure of Structure of the Rhodium Mesoporphyrin IX-Reconstituted CYP102A1 Haem Domain with N-Abietoyl-L-Tryptophan, PDB code: 6k24 was solved by J.K.Stanfield, A.Matsumoto, 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)	48.74 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	59.082, 149.182, 65.213, 90.00, 99.76, 90.00
R / Rfree (%)	20.8 / 25.6

The binding sites of Rhodium atom in the Structure of the Rhodium Mesoporphyrin IX-Reconstituted CYP102A1 Haem Domain with N-Abietoyl-L-Tryptophan (pdb code 6k24). This binding sites where shown within 5.0 Angstroms radius around Rhodium atom.
In total 2 binding sites of Rhodium where determined in the Structure of the Rhodium Mesoporphyrin IX-Reconstituted CYP102A1 Haem Domain with N-Abietoyl-L-Tryptophan, PDB code: 6k24:
Jump to Rhodium binding site number: 1; 2;

Rhodium binding site 1 out of 2 in the Structure of the Rhodium Mesoporphyrin IX-Reconstituted CYP102A1 Haem Domain with N-Abietoyl-L-Tryptophan


Mono view


Stereo pair view

A full contact list of Rhodium with other atoms in the Rh binding site number 1 of Structure of the Rhodium Mesoporphyrin IX-Reconstituted CYP102A1 Haem Domain with N-Abietoyl-L-Tryptophan within 5.0Å range: probe atom residue distance (Å) B Occ A:Rh502 b:30.0 occ:1.00 RH A:CV0502 0.0 30.0 1.0 NB A:CV0502 2.1 26.0 1.0 ND A:CV0502 2.1 26.3 1.0 NA A:CV0502 2.1 28.3 1.0 NC A:CV0502 2.1 27.1 1.0 SG A:CYS400 2.3 28.0 1.0 S A:DMS503 2.3 33.9 1.0 C4A A:CV0502 3.0 29.2 1.0 C1D A:CV0502 3.0 28.0 1.0 C4B A:CV0502 3.1 27.4 1.0 C4C A:CV0502 3.1 29.1 1.0 C1C A:CV0502 3.1 27.7 1.0 C4D A:CV0502 3.1 30.5 1.0 C1B A:CV0502 3.1 29.3 1.0 C1A A:CV0502 3.1 31.3 1.0 O A:DMS503 3.1 64.1 1.0 CB A:CYS400 3.2 33.6 1.0 CHB A:CV0502 3.4 27.5 1.0 CHD A:CV0502 3.5 28.2 1.0 CHC A:CV0502 3.5 27.2 1.0 C1 A:DMS503 3.5 39.5 1.0 CHA A:CV0502 3.5 29.4 1.0 C2 A:DMS503 3.5 38.7 1.0 CA A:CYS400 4.0 34.4 1.0 C2D A:CV0502 4.3 29.4 1.0 C3C A:CV0502 4.3 30.4 1.0 C3B A:CV0502 4.3 29.1 1.0 C3A A:CV0502 4.3 30.9 1.0 C3D A:CV0502 4.3 29.9 1.0 C2C A:CV0502 4.3 32.9 1.0 C2A A:CV0502 4.3 31.9 1.0 C2B A:CV0502 4.3 28.6 1.0 CB A:ALA264 4.8 37.5 1.0 C A:CYS400 4.9 33.6 1.0 N A:GLY402 4.9 34.0 1.0

Rhodium binding site 2 out of 2 in the Structure of the Rhodium Mesoporphyrin IX-Reconstituted CYP102A1 Haem Domain with N-Abietoyl-L-Tryptophan


Mono view


Stereo pair view

A full contact list of Rhodium with other atoms in the Rh binding site number 2 of Structure of the Rhodium Mesoporphyrin IX-Reconstituted CYP102A1 Haem Domain with N-Abietoyl-L-Tryptophan within 5.0Å range: probe atom residue distance (Å) B Occ B:Rh502 b:33.3 occ:1.00 RH B:CV0502 0.0 33.3 1.0 ND B:CV0502 2.1 25.4 1.0 NB B:CV0502 2.2 29.3 1.0 NA B:CV0502 2.2 31.7 1.0 NC B:CV0502 2.2 28.2 1.0 SG B:CYS400 2.2 28.9 1.0 S B:DMS503 2.3 33.2 1.0 O B:DMS503 3.0 54.0 1.0 C1D B:CV0502 3.0 29.0 1.0 C4D B:CV0502 3.1 29.5 1.0 C4B B:CV0502 3.1 31.6 1.0 C4C B:CV0502 3.1 28.8 1.0 C4A B:CV0502 3.1 32.4 1.0 C1C B:CV0502 3.1 27.2 1.0 C1A B:CV0502 3.2 29.2 1.0 C1B B:CV0502 3.2 34.5 1.0 CB B:CYS400 3.3 32.9 1.0 CHD B:CV0502 3.5 26.3 1.0 CHC B:CV0502 3.5 29.4 1.0 C1 B:DMS503 3.5 41.6 1.0 CHA B:CV0502 3.5 28.1 1.0 CHB B:CV0502 3.5 29.7 1.0 C2 B:DMS503 3.5 38.1 1.0 CA B:CYS400 4.0 32.8 1.0 C2D B:CV0502 4.2 30.1 1.0 C3D B:CV0502 4.3 30.4 1.0 C3C B:CV0502 4.3 29.5 1.0 C3A B:CV0502 4.3 28.4 1.0 C3B B:CV0502 4.3 29.8 1.0 C2C B:CV0502 4.4 31.3 1.0 C2A B:CV0502 4.4 28.4 1.0 C2B B:CV0502 4.5 33.4 1.0 C B:CYS400 4.9 34.1 1.0 CB B:ALA264 4.9 34.0 0.5 CB B:ALA264 4.9 36.2 0.5

O.Shoji, J.K.Stanfield. Structure of the Rhodium Mesoporphyrin IX-Reconstituted CYP102A1 Haem Domain with N-Abietoyl-L-Tryptophan at 2.10 Angstroms Resolution To Be Published.