Structure of PDB 1uoo Chain A

Receptor sequence
>1uooA (length=710) Species: 9823 (Sus scrofa) [Search protein sequence]
MLSFQYPDVYRDETAIQDYHGHKVCDPYAWLEDPDSEQTKAFVEAQNKIT
VPFLEQCPIRGLYKERMTELYDYPKYSCHFKKGKRYFYFYNTGLQNQRVL
YVQDSLEGEARVFLDPNILSDDGTVALRGYAFSEDGEYFAYGLSASGSDW
VTIKFMKVDGAKELPDVLERVKFSCMAWTHDGKGMFYNAYPQQDGKSDGT
ETSTNLHQKLYYHVLGTDQSEDILCAEFPDEPKWMGGAELSDDGRYVLLS
IREGCDPVNRLWYCDLQQESNGITGILKWVKLIDNFEGEYDYVTNEGTVF
TFKTNRHSPNYRLINIDFTDPEESKWKVLVPEHEKDVLEWVACVRSNFLV
LCYLHDVKNTLQLHDLATGALLKIFPLEVGSVVGYSGQKKDTEIFYQFTS
FLSPGIIYHCDLTKEELEPRVFREVTVKGIDASDYQTVQIFYPSKDGTKI
PMFIVHKKGIKLDGSHPAFLYGYGGFNISITPNYSVSRLIFVRHMGGVLA
VANIRGGGEYGETWHKGGILANKQNCFDDFQCAAEYLIKEGYTSPKRLTI
NGGANGGLLVATCANQRPDLFGCVIAQVGVMDMLKFHKYTIGHAWTTDYG
CSDSKQHFEWLIKYSPLHNVKLPEADDIQYPSMLLLTADHDDRVVPLHSL
KFIATLQYIVGRSRKQNNPLLIHVDTKAGHGAGKPTAKVIEEVSDMFAFI
ARCLNIDWIP
3D structure
PDB1uoo Electrostatic Environment at the Active Site of Prolyl Oligopeptidase is Highly Influential During Substrate Binding
ChainA
Resolution2.35 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 A554 D641 H680
Catalytic site (residue number reindexed from 1) Y473 A554 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 peptide A F173 M235 Y473 F476 A554 N555 W595 R643 F173 M235 Y473 F476 A554 N555 W595 R643
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:1uoo, PDBe:1uoo, PDBj:1uoo
PDBsum1uoo
PubMed14514675
UniProtP23687|PPCE_PIG Prolyl endopeptidase (Gene Name=PREP)

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