Structure of PDB 5jmo Chain A

Receptor sequence

>5jmoA (length=469) Species: 9606 (Homo sapiens)

YQEPTDPKFPQQWYLSGVTQRDLNVKAAWAQGYTGHGIVVSILDDGIEKN
HPDLAGNYDPGASFDVNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNG
VCGVGVAYNARIGGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPEDD
GKTVDGPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYT
NSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNEKQIVTTDLRQK
CTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSKPAHLNAN
DWATNGVGRKVSHSYGYGLLDAGAMVALAQNWTTVAPQRKCIIDILTEPK
DIGKRLEVRKTVTACLGEPNHITRLEHAQARLTLSYNRRGDLAIHLVSPM
GTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWVLEIENTSEANN
YGTLTKFTLVLYGTASGSL

3D structure

• PDB: 5jmo The structure of a furin-antibody complex explains non-competitive inhibition by steric exclusion of substrate conformers.
• Chain: A
• Resolution: 1.998 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): S150 D191
• Catalytic site (residue number reindexed from 1): S41 D82
• 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	A	D154 H194 E236 S253 W254 G255 P256 D258 D264 G294 N295 D306 Y308 S368	D45 H85 E127 S144 W145 G146 P147 D149 D155 G185 N186 D197 Y199 S259
BS02	peptide	A	H194 S368	H85 S259
BS03	CA	A	D174 D179 D181	D65 D70 D72
BS04	CA	A	D115 D162 V205 N208 V210 G212	D6 D53 V96 N99 V101 G103
BS05	CA	A	D258 D301 E331	D149 D192 E222

Gene Ontology

Molecular Function

• GO:0004252 serine-type endopeptidase activity
• GO:0008236 serine-type peptidase activity

Biological Process

• GO:0006508 proteolysis

External links

• PDB: RCSB:5jmo, PDBe:5jmo, PDBj:5jmo
• PDBsum: 5jmo
• PubMed: 27670069
• UniProt: P09958|FURIN_HUMAN Furin (Gene Name=FURIN)