Factor viia in complex with the inhibitor 1-[(2R,15R)-2-[(1-amino-4- fluoroisoquinolin-6-YL)AMINO]-4,15,20-trimethyl-3,12-dioxo-13-oxa-4, 11-DIAZATRICYCLO[14.2.2.1~6,10~]HENICOSA-1(18),6,8,10(21),16,19- hexaen-7-yl] cyclobutane-1-carboxylic acid

Structure

x-ray diffraction · 2 distinct chains · 15% helix, 35% strand (DSSP).

Ligands and binding sites

• 70D · 1-[(2R,15R)-2-[(1-amino-4-fluoroisoquinolin-6-yl) amino]-4,15,17-trimethyl-3,12-dioxo-13-oxa-4,11-diazatricyclo[14.2.2.1~6,10~]henicosa-1(18),6(21),7,9, 16,19-hexaen-7-yl]cyclobutane-1-carboxylic acid · ligand · chains H
• CA · Calcium ion · metal · chains H
• SO4 · Sulfate ion · ion · 4 copies · chains H, L
• GOL · Glycerol · additive · 2 copies · chains H, L

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• H–L · 1055 Ų buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

• 5L2Y · Factor VIIa in complex with the inhibitor 1-[(2R,15R)-2-[(1-amino-4-fluoroisoquinolin-6-yl… · the same entry in another collection · chain H against H, TM-score 1.00
• P08709 · AlphaFold monomer V2.0 prediction for coagulation factor VII (P08709) · a predicted model of the same protein · chain H against A, TM-score 0.97

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 P08709
• Elsewhere: RCSB PDB 5L2Y · PDBe 5L2Y · UniProt P08709