Structure of the carbonylruthenium mesoporphyrin IX-reconstituted CYP102A1 haem domain with N-abietoyl-L-tryptophan

Structure

x-ray diffraction · 2 distinct chains · 54% helix, 11% strand (DSSP).

Ligands and binding sites

• RUR · [3,3'-(7,12-diethyl-3,8,13,17-tetramethylporphyrin-2, 18-diyl-kappa~4~n~21~,n~22~,n~23~,n~24~) dipropanoato(2-)]ruthenium · ligand · 2 copies · chains A, B
• WAA · (2S)-2-[[(1R,4aR,4bR,10aR)-1,4a-dimethyl-7-propan-2-yl-2,3,4,4b,5,6,10,10a-octahydrophenanthren-1-yl]carbonylamino]-3-( 1H-indol-3-yl)propanoic acid · ligand · 2 copies · chains A, B
• CMO · Carbon monoxide · ion · 2 copies · chains A, B
• GOL · Glycerol · additive · 13 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 923 Ų buried · 14 hydrogen bonds · protein-protein

Compared structures

• 6K9S · Structure of the Carbonylruthenium Mesoporphyrin IX-Reconstituted CYP102A1 Haem Domain… · the same entry in another collection · chain A against A, TM-score 1.00
• P14779 · AlphaFold monomer V2.0 prediction for bifunctional cytochrome P450/NADPH--P450 reductase… · a predicted model of the same protein · chain B against A, TM-score 0.98

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P14779
• Elsewhere: RCSB PDB 6K9S · PDBe 6K9S · UniProt P14779