Structure of PDB 1qfm Chain A

Receptor sequence
>1qfmA (length=710) Species: 9823 (Sus scrofa) [Search protein sequence]
MLSFQYPDVYRDETAIQDYHGHKVCDPYAWLEDPDSEQTKAFVEAQNKIT
VPFLEQCPIRGLYKERMTELYDYPKYSCHFKKGKRYFYFYNTGLQNQRVL
YVQDSLEGEARVFLDPNILSDDGTVALRGYAFSEDGEYFAYGLSASGSDW
VTIKFMKVDGAKELPDVLERVKFSCMAWTHDGKGMFYNAYPQQDGKSDGT
ETSTNLHQKLYYHVLGTDQSEDILCAEFPDEPKWMGGAELSDDGRYVLLS
IREGCDPVNRLWYCDLQQESNGITGILKWVKLIDNFEGEYDYVTNEGTVF
TFKTNRHSPNYRLINIDFTDPEESKWKVLVPEHEKDVLEWVACVRSNFLV
LCYLHDVKNTLQLHDLATGALLKIFPLEVGSVVGYSGQKKDTEIFYQFTS
FLSPGIIYHCDLTKEELEPRVFREVTVKGIDASDYQTVQIFYPSKDGTKI
PMFIVHKKGIKLDGSHPAFLYGYGGFNISITPNYSVSRLIFVRHMGGVLA
VANIRGGGEYGETWHKGGILANKQNCFDDFQCAAEYLIKEGYTSPKRLTI
NGGSNGGLLVATCANQRPDLFGCVIAQVGVMDMLKFHKYTIGHAWTTDYG
CSDSKQHFEWLIKYSPLHNVKLPEADDIQYPSMLLLTADHDDRVVPLHSL
KFIATLQYIVGRSRKQNNPLLIHVDTKAGHGAGKPTAKVIEEVSDMFAFI
ARCLNIDWIP
3D structure
PDB1qfm Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis.
ChainA
Resolution1.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y473 S554 D641 H680
Catalytic site (residue number reindexed from 1) Y473 S554 D641 H680
Enzyme Commision number 3.4.21.26: prolyl oligopeptidase.
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 SGL A Y473 S554 N555 H680 Y473 S554 N555 H680
BS02 SGL A M235 I591 M235 I591
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
GO:0070012 oligopeptidase activity
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1qfm, PDBe:1qfm, PDBj:1qfm
PDBsum1qfm
PubMed9695945
UniProtP23687|PPCE_PIG Prolyl endopeptidase (Gene Name=PREP)

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