Structure of PDB 4ryd Chain F

Receptor sequence
>4rydF (length=465) Species: 9606 (Homo sapiens) [Search protein sequence]
YQEPTDPKFPQQWYLSGVTQRDLNVKAAWAQGYTGHGIVVSILDDGIEKN
HPDLAGNYDPGASFDVNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNG
VCGVGVAYNARIGGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPEDD
GKTVDGPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYT
NSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNEKQIVTTDLRQK
CTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSKPAHLNAN
DWATNGVGRKVSHSYGYGLLDAGAMVALAQNWTTVAPQRKCIIDILTEPK
DIGKRLEVRKTVTACLGEPNHITRLEHAQARLTLSYNRRGDLAIHLVSPM
GTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWVLEIENTSEANN
YGTLTKFTLVLYGTA
3D structure
PDB4ryd Novel Furin Inhibitors with Potent Anti-infectious Activity.
ChainF
Resolution2.15 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) D44 H85
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 F D154 H194 V231 E236 W254 G255 P256 D264 Y308 D45 H85 V122 E127 W145 G146 P147 D155 Y199
BS02 CA F D115 D162 V205 N208 V210 G212 D6 D53 V96 N99 V101 G103
BS03 CA F D258 D301 E331 D149 D192 E222
BS04 CA F D174 D179 D181 D65 D70 D72
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:4ryd, PDBe:4ryd, PDBj:4ryd
PDBsum4ryd
PubMed25974265
UniProtP09958|FURIN_HUMAN Furin (Gene Name=FURIN)

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