Structure of PDB 5vlh Chain A

Receptor sequence
>5vlhA (length=355) Species: 9606 (Homo sapiens) [Search protein sequence]
TATFHRCAKDPWRLPGTYVVVLKEETHLSQSERTARRLQAQAARRGYLTK
ILHVFHGLLPGFLVKMSGDLLELALKLPHVDYIEEDSSVFAQGGSLVEVY
LLDTSIQSDHREIEGRVMVTDFENVPEEDSKCDSHGTHLAGVVSGRDAGV
AKGASMRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLLPLAG
GYSRVLNAACQRLARAGVVLVTAAGNFRDDACLYSPASAPEVITVGATNA
QDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSQSGTSQAAAH
VAGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLV
AALPP
3D structure
PDB5vlh Discovery of a cryptic peptide-binding site on PCSK9 and design of antagonists.
ChainA
Resolution2.86 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) D103 H135 N226 S295
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 A A239 N340 A341 P364 E366 D367 I368 I369 H391 A443 L444 A148 N249 A250 P273 E275 D276 I277 I278 H300 A352 L353
BS02 peptide A D238 A239 I369 T377 C378 F379 V380 D147 A148 I278 T286 C287 F288 V289
BS03 CA A P331 V333 D360 P240 V242 D269
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:5vlh, PDBe:5vlh, PDBj:5vlh
PDBsum5vlh
PubMed28825733
UniProtQ8NBP7|PCSK9_HUMAN Proprotein convertase subtilisin/kexin type 9 (Gene Name=PCSK9)

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