Structure of PDB 4ne9 Chain B

Receptor sequence
>4ne9B (length=490) Species: 9606 (Homo sapiens) [Search protein sequence]
SIPWNLERITPPRYRAGGSLVEVYLLDTSIQSDHREIEGRVMVTDFENVP
EEDQASKCDSHGTHLAGVVSGRDAGVAKGASMRSLRVLNCQGKGTVSGTL
IGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLVTAA
GNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPG
EDIIGASSDCSTCFVSQSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRL
IHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHQLFCRTVWSAHSGPTR
MATAIARCAPDEELLSCSSFSRSGKRRGERMEAQGGKLVCRAHNAFGGEG
VYAIARCCLLPQANCSVHTAPPAEASMGTRVHCHQQGHVLTGCSSHWEVE
DLGPNQCVGHREASIHASCCHAPGLECKVKEHGIPAPQEQVTVACEEGWT
LTGCSALPGTSHVLGAYAVDNTCVVRSRAVTAVAICCRSR
3D structure
PDB4ne9 Design and synthesis of truncated EGF-A peptides that restore LDL-R recycling in the presence of PCSK9 in vitro.
ChainB
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D186 H226 N317 S386
Catalytic site (residue number reindexed from 1) D27 H61 N152 S221
Enzyme Commision number 3.4.21.-
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 R194 I369 C375 T377 C378 F379 V380 R35 I204 C210 T212 C213 F214 V215
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:4ne9, PDBe:4ne9, PDBj:4ne9
PDBsum4ne9
PubMed24440079
UniProtQ8NBP7|PCSK9_HUMAN Proprotein convertase subtilisin/kexin type 9 (Gene Name=PCSK9)

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