Crystal Structure of Factor VIIa in complex with 1-(1-aminoisoquinolin-6-yl)-3-benzylurea

Crystal Structure of a Factor VIIa complex

Proconvertin,Serum prothrombin conversion accelerator,SPCA

IVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPS
TYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQ
QSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMR
SEPRPGVLLRAPFP

16 mg/ml protein in 20mM Tris/HCl pH 8.4, 5 mM benzamidine, 0.1 M NaCl, 50 mM CaCl2 mixed 1+1 with 32-35% AMMONIUM SULPHATE, 2% PEG 4000, 0.1 M Bicine-NaOH pH 8.5, 15% glycerol

Crystal Structures of Factor VIIa Complexes

the numbering follows that of the unprocessed precursor ARG A 204 ILE A 213 gap ALA A 375 SER A 380 gap main-chain flexibility K401-G402 ligand entertains three h-bonds, two with D398 and one with S404. phenyl moiety of ligand is flexible according to weaker density compared to rest of ligand but stacks against H225. very good overlay of benzamidine and 1-amino-isoquinoline over all atoms of benzamidine. an unfavorable interaction between 1-amino-isoquinoline and the carbonyl group of G427 exists.. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

GLYCOPROTEIN, HYDROLASE, SERINE PROTEASE, PLASMA, BLOOD COAGULATION FACTOR, PROTEIN INHIBITOR COMPLEX, CALCIUM-BINDING, HYDROLASE-HYDROLASE INHIBITOR COMPLEX