Structure of PDB 5jxg Chain A

Receptor sequence
>5jxgA (length=473) Species: 9606 (Homo sapiens) [Search protein sequence]
VYQEPTDPKFPQQWYLSGVTQRDLNVKAAWAQGYTGHGIVVSILDDGIEK
NHPDLAGNYDPGASFDVNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANN
GVCGVGVAYNARIGGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPED
DGKTVDGPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGY
TNSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNEKQIVTTDLRQ
KCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSKPAHLNA
NDWATNGVGRKVSHSYGYGLLDAGAMVALAQNWTTVAPQRKCIIDILTEP
KDIGKRLEVRKTVTACLGEPNHITRLEHAQARLTLSYNRRGDLAIHLVSP
MGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWVLEIENTSEAN
NYGTLTKFTLVLYGTASGSLVPR
3D structure
PDB5jxg Structure of the unliganded form of the proprotein convertase furin suggests activation by a substrate-induced mechanism.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D153 H194
Catalytic site (residue number reindexed from 1) D45 H86
Enzyme Commision number 3.4.21.75: furin.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CA A D174 D179 D181 D66 D71 D73
BS02 CA A D115 D162 V205 N208 V210 G212 D7 D54 V97 N100 V102 G104
BS03 CA A D258 D301 E331 D150 D193 E223
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:5jxg, PDBe:5jxg, PDBj:5jxg
PDBsum5jxg
PubMed27647913
UniProtP09958|FURIN_HUMAN Furin (Gene Name=FURIN)

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