Ruthenium in PDB 6k9s: Structure of the Carbonylruthenium Mesoporphyrin IX-Reconstituted CYP102A1 Haem Domain with N-Abietoyl-L-Tryptophan

All present enzymatic activity of Structure of the Carbonylruthenium 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 Carbonylruthenium Mesoporphyrin IX-Reconstituted CYP102A1 Haem Domain with N-Abietoyl-L-Tryptophan, PDB code: 6k9s was solved by J.K.Stanfield, K.Omura, 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)	46.49 / 1.55
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	59.116, 128.556, 149.452, 90.00, 90.00, 90.00
R / Rfree (%)	16.7 / 20.5

The binding sites of Ruthenium atom in the Structure of the Carbonylruthenium Mesoporphyrin IX-Reconstituted CYP102A1 Haem Domain with N-Abietoyl-L-Tryptophan (pdb code 6k9s). This binding sites where shown within 5.0 Angstroms radius around Ruthenium atom.
In total 2 binding sites of Ruthenium where determined in the Structure of the Carbonylruthenium Mesoporphyrin IX-Reconstituted CYP102A1 Haem Domain with N-Abietoyl-L-Tryptophan, PDB code: 6k9s:
Jump to Ruthenium binding site number: 1; 2;

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


Mono view


Stereo pair view

A full contact list of Ruthenium with other atoms in the Ru binding site number 1 of Structure of the Carbonylruthenium Mesoporphyrin IX-Reconstituted CYP102A1 Haem Domain with N-Abietoyl-L-Tryptophan within 5.0Å range: probe atom residue distance (Å) B Occ A:Ru501 b:18.9 occ:1.00 RU A:RUR501 0.0 18.9 1.0 C A:CMO502 1.8 18.3 1.0 NB A:RUR501 2.1 18.2 1.0 ND A:RUR501 2.1 18.1 1.0 NA A:RUR501 2.1 17.5 1.0 NC A:RUR501 2.1 18.7 1.0 SG A:CYS400 2.4 19.8 1.0 O A:CMO502 2.9 24.4 1.0 C1B A:RUR501 3.0 17.7 1.0 C1C A:RUR501 3.1 19.0 1.0 C4C A:RUR501 3.1 18.5 1.0 C1D A:RUR501 3.1 16.9 1.0 C4B A:RUR501 3.1 16.6 1.0 C4D A:RUR501 3.1 18.3 1.0 C1A A:RUR501 3.1 18.1 1.0 C4A A:RUR501 3.2 17.8 1.0 CHC A:RUR501 3.4 19.0 1.0 CHB A:RUR501 3.5 19.6 1.0 CHD A:RUR501 3.5 19.4 1.0 CB A:CYS400 3.5 18.7 1.0 CHA A:RUR501 3.5 17.8 1.0 CA A:CYS400 4.2 18.8 1.0 C3C A:RUR501 4.3 21.6 1.0 C2B A:RUR501 4.3 19.2 1.0 C2D A:RUR501 4.3 17.6 1.0 C2C A:RUR501 4.3 21.0 1.0 C3B A:RUR501 4.4 18.5 1.0 C3D A:RUR501 4.4 17.9 1.0 C2A A:RUR501 4.4 17.0 1.0 C3A A:RUR501 4.4 18.1 1.0 CE2 A:PHE87 4.5 26.6 1.0 O A:ALA264 4.5 26.0 1.0 CB A:ALA264 4.8 25.1 1.0 OG1 A:THR268 4.9 27.1 1.0 CD2 A:PHE87 5.0 24.7 1.0

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


Mono view


Stereo pair view

A full contact list of Ruthenium with other atoms in the Ru binding site number 2 of Structure of the Carbonylruthenium Mesoporphyrin IX-Reconstituted CYP102A1 Haem Domain with N-Abietoyl-L-Tryptophan within 5.0Å range: probe atom residue distance (Å) B Occ B:Ru501 b:19.7 occ:1.00 RU B:RUR501 0.0 19.7 1.0 C B:CMO502 1.7 25.0 1.0 NA B:RUR501 2.1 18.9 1.0 ND B:RUR501 2.1 18.6 1.0 NC B:RUR501 2.2 19.7 1.0 NB B:RUR501 2.2 20.0 1.0 SG B:CYS400 2.4 20.3 1.0 O B:CMO502 2.8 25.9 1.0 C1D B:RUR501 3.1 17.6 1.0 C1B B:RUR501 3.1 19.3 1.0 C4B B:RUR501 3.1 19.6 1.0 C4D B:RUR501 3.1 20.0 1.0 C1C B:RUR501 3.1 21.6 1.0 C4C B:RUR501 3.1 18.6 1.0 C1A B:RUR501 3.1 18.2 1.0 C4A B:RUR501 3.1 18.8 1.0 CHC B:RUR501 3.5 20.6 1.0 CHA B:RUR501 3.5 20.3 1.0 CHD B:RUR501 3.5 20.4 1.0 CHB B:RUR501 3.5 20.0 1.0 CB B:CYS400 3.5 20.2 1.0 CA B:CYS400 4.2 20.2 1.0 C2D B:RUR501 4.4 20.1 1.0 C2B B:RUR501 4.4 20.9 1.0 C3B B:RUR501 4.4 20.4 1.0 C2A B:RUR501 4.4 19.6 1.0 C3A B:RUR501 4.4 18.9 1.0 C2C B:RUR501 4.4 21.3 1.0 C3C B:RUR501 4.4 21.5 1.0 C3D B:RUR501 4.4 18.2 1.0 CE2 B:PHE87 4.4 26.0 1.0 O B:ALA264 4.5 27.5 1.0 CB B:ALA264 4.8 29.3 1.0 CD2 B:PHE87 4.9 25.2 1.0 OG1 B:THR268 5.0 26.9 1.0 N B:GLY402 5.0 20.2 1.0

O.Shoji, J.K.Stanfield. Structure of the Carbonylruthenium Mesoporphyrin IX-Reconstituted CYP102A1 Haem Domain with N-Abietoyl-L-Tryptophan at 1.55 Angstrom Resolution To Be Published.