Molybdenum in PDB 6jmh: Structure of the Oxomolybdenum Mesoporphyrin IX-Reconstituted CYP102A1 Haem Domain with N-Abietoyl-L-Tryptophan

All present enzymatic activity of Structure of the Oxomolybdenum 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 Oxomolybdenum Mesoporphyrin IX-Reconstituted CYP102A1 Haem Domain with N-Abietoyl-L-Tryptophan, PDB code: 6jmh 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)	48.08 / 1.46
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	58.967, 148.910, 63.536, 90.00, 98.34, 90.00
R / Rfree (%)	12.6 / 16.8

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

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


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Structure of the Oxomolybdenum Mesoporphyrin IX-Reconstituted CYP102A1 Haem Domain with N-Abietoyl-L-Tryptophan within 5.0Å range: probe atom residue distance (Å) B Occ A:Mo501 b:16.1 occ:1.00 MO A:MI9501 0.0 16.1 1.0 O A:MI9501 1.8 18.0 1.0 N24 A:MI9501 2.1 14.1 1.0 N37 A:MI9501 2.1 13.1 1.0 N31 A:MI9501 2.1 13.7 1.0 N14 A:MI9501 2.1 14.8 1.0 SG A:CYS400 2.7 15.3 1.0 C23 A:MI9501 3.1 14.8 1.0 C03 A:MI9501 3.1 14.5 1.0 C15 A:MI9501 3.1 15.8 1.0 C21 A:MI9501 3.1 14.7 1.0 C17 A:MI9501 3.1 15.7 1.0 C05 A:MI9501 3.1 14.8 1.0 C28 A:MI9501 3.1 14.5 1.0 C30 A:MI9501 3.1 14.2 1.0 C22 A:MI9501 3.4 14.5 1.0 C16 A:MI9501 3.4 16.0 1.0 C04 A:MI9501 3.4 14.3 1.0 C29 A:MI9501 3.5 15.1 1.0 CB A:CYS400 3.6 14.4 1.0 CE2 A:PHE87 4.1 21.8 0.5 C25 A:MI9501 4.3 14.6 1.0 C02 A:MI9501 4.3 16.0 1.0 C40 A:MI9501 4.3 16.7 1.0 C18 A:MI9501 4.3 16.1 1.0 C20 A:MI9501 4.3 16.8 1.0 C27 A:MI9501 4.3 16.0 1.0 C06 A:MI9501 4.3 14.7 1.0 CA A:CYS400 4.4 13.7 1.0 C08 A:MI9501 4.4 15.3 1.0 CB A:ALA264 4.5 22.5 1.0 CD2 A:PHE87 4.7 16.5 0.5 CG2 A:THR268 4.9 20.9 0.3

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


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of Structure of the Oxomolybdenum Mesoporphyrin IX-Reconstituted CYP102A1 Haem Domain with N-Abietoyl-L-Tryptophan within 5.0Å range: probe atom residue distance (Å) B Occ B:Mo501 b:15.9 occ:1.00 MO B:MI9501 0.0 15.9 1.0 O B:MI9501 1.8 18.3 1.0 N31 B:MI9501 2.1 13.7 1.0 N14 B:MI9501 2.1 12.4 1.0 N24 B:MI9501 2.1 13.0 1.0 N37 B:MI9501 2.1 11.9 1.0 SG B:CYS400 2.7 15.3 1.0 C15 B:MI9501 3.1 15.2 1.0 C03 B:MI9501 3.1 14.1 1.0 C05 B:MI9501 3.1 13.7 1.0 C23 B:MI9501 3.1 13.8 1.0 C17 B:MI9501 3.1 13.8 1.0 C30 B:MI9501 3.1 13.4 1.0 C21 B:MI9501 3.1 14.9 1.0 C28 B:MI9501 3.1 14.4 1.0 C16 B:MI9501 3.4 15.0 1.0 C04 B:MI9501 3.5 14.5 1.0 C29 B:MI9501 3.5 13.9 1.0 C22 B:MI9501 3.5 14.7 1.0 CB B:CYS400 3.7 15.2 1.0 CE2 B:PHE87 4.2 20.3 0.5 C40 B:MI9501 4.3 15.2 1.0 C02 B:MI9501 4.3 14.8 1.0 C25 B:MI9501 4.3 14.1 1.0 C20 B:MI9501 4.3 16.6 1.0 C18 B:MI9501 4.3 15.6 1.0 C06 B:MI9501 4.3 14.4 1.0 C27 B:MI9501 4.4 15.2 1.0 CA B:CYS400 4.4 14.4 1.0 C08 B:MI9501 4.4 14.1 1.0 CB B:ALA264 4.5 23.0 1.0 CD2 B:PHE87 4.8 19.8 0.5 CG2 B:THR268 4.8 34.7 0.7

O.Shoji, J.K.Stanfield. Structure of Oxomolybdenum Mesoporphyrin IX-Reconstituted CYP102A1 Haem Domain with N-Abietoyl-L-Tryptophan at 1.46 Angstrom Resolution To Be Published.