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Ligands
Code Name Style Show Link
CA Calcium ion
CL Chloride ion
NA Sodium ion
Non-standard Residues
Code Name Show
Glycosylation
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Modification
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00S 4-(aminomethyl)benzenecarboximidamide
2UC 1-[3-(2-oxoethyl)benzyl]guanidine
Code : 5JXH   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Structure the proprotein convertase furin in complex with meta-guanidinomethyl-Phac-RVR-Amba at 2.0 Angstrom resolution.
Release Data : 2016-10-05
Compound :
mol_id molecule chains synonym
1 Furin A Dibasic-processing enzyme,Paired basic amino acid residue-cleaving enzyme,PACE
ec: 3.4.21.75
mol_id molecule chains
2 2UC-ARG-VAL-ARG-00S H
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Homo sapiens  (taxid:9606)
gene: FURIN, FUR, PACE, PCSK3
expression_system_common: Human
expression_system_cell_line: HEK293
mol_id organism_scientific
2 Synthetic construct  (taxid:32630)
synthetic: yes
Authors : Dahms, S.O., Arciniega, M., Steinmetzer, T., Huber, R., Than, M.E.
Keywords : protease, inhibitor, proteolysis, hydrolase
Exp. method : X-RAY DIFFRACTION ( 2.000 Å )
Citation :

Structure of the unliganded form of the proprotein convertase furin suggests activation by a substrate-induced mechanism.

Dahms, S.O.,Arciniega, M.,Steinmetzer, T.  et al.
(2016)  Proc.Natl.Acad.Sci.USA  113 : 11196 - 11201

PubMed: 27647913
DOI: 10.1073/pnas.1613630113

Chain : A
UniProt : P09958 (FURIN_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
Release of mature proteins from their proproteins by cleavage of -Arg-Xaa-Yaa-Arg-|-Zaa- bonds, where Xaa can be any amino acid and Yaa is Arg or Lys. Releases albumin, complement component C3 and von Willebrand factor from their respective precursors. 3.4.21.75 PubMed:11799113, PubMed:1438214, PubMed:1629222, PubMed:1644824, PubMed:1713771, PubMed:2251280, PubMed:24666235, PubMed:25974265, PubMed:31091448, PubMed:32362314, PubMed:32703818, PubMed:7592877, PubMed:7690548, PubMed:7737999, PubMed:8253774, PubMed:9130696
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