Structure of PDB 5jmo Chain B

Receptor sequence
>5jmoB (length=471) Species: 9606 (Homo sapiens) [Search protein sequence]
DVYQEPTDPKFPQQWYLSGVTQRDLNVKAAWAQGYTGHGIVVSILDDGIE
KNHPDLAGNYDPGASFDVNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVAN
NGVCGVGVAYNARIGGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPE
DDGKTVDGPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDG
YTNSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNEKQIVTTDLR
QKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSKPAHLN
ANDWATNGVGRKVSHSYGYGLLDAGAMVALAQNWTTVAPQRKCIIDILTE
PKDIGKRLEVRKTVTACLGEPNHITRLEHAQARLTLSYNRRGDLAIHLVS
PMGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWVLEIENTSEA
NNYGTLTKFTLVLYGTASGSL
3D structure
PDB5jmo The structure of a furin-antibody complex explains non-competitive inhibition by steric exclusion of substrate conformers.
ChainB
Resolution1.998 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S150 D191
Catalytic site (residue number reindexed from 1) S43 D84
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 peptide B D154 H194 E236 S253 W254 G255 E257 D258 D264 G294 N295 D306 Y308 S368 D47 H87 E129 S146 W147 G148 E150 D151 D157 G187 N188 D199 Y201 S261
BS02 CA B D174 D179 D181 D67 D72 D74
BS03 CA B D115 D162 V205 N208 V210 G212 D8 D55 V98 N101 V103 G105
BS04 CA B D258 D301 E331 D151 D194 E224
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

View graph for
Biological Process
External links
PDB RCSB:5jmo, PDBe:5jmo, PDBj:5jmo
PDBsum5jmo
PubMed27670069
UniProtP09958|FURIN_HUMAN Furin (Gene Name=FURIN)

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