Structure of PDB 1h2y Chain A

Receptor sequence
>1h2yA (length=710) Species: 9823 (Sus scrofa) [Search protein sequence]
MLSFQYPDVYRDETAIQDYHGHKVCDPYAWLEDPDSEQTKAFVEAQNKIT
VPFLEQCPIRGLYKERMTELYDYPKYSCHFKKGKRYFYFYNTGLQNQRVL
YVQDSLEGEARVFLDPNILSDDGTVALRGYAFSEDGEYFAYGLSASGSDW
VTIKFMKVDGAKELPDVLERVKFSCMAWTHDGKGMFYNAYPQQDGKSDGT
ETSTNLHQKLYYHVLGTDQSEDILCAEFPDEPKWMGGAELSDDGRYVLLS
IREGCDPVNRLWYCDLQQESNGITGILKWVKLIDNFEGEYDYVTNEGTVF
TFKTNRHSPNYRLINIDFTDPEESKWKVLVPEHEKDVLEWVACVRSNFLV
LCYLHDVKNTLQLHDLATGALLKIFPLEVGSVVGYSGQKKDTEIFYQFTS
FLSPGIIYHCDLTKEELEPRVFREVTVKGIDASDYQTVQIFYPSKDGTKI
PMFIVHKKGIKLDGSHPAFLYGFGGFNISITPNYSVSRLIFVRHMGGVLA
VANIRGGGEYGETWHKGGILANKQNCFDDFQCAAEYLIKEGYTSPKRLTI
NGGSNGGLLVATCANQRPDLFGCVIAQVGVMDMLKFHKYTIGHAWTTDYG
CSDSKQHFEWLIKYSPLHNVKLPEADDIQYPSMLLLTADHDDRVVPLHSL
KFIATLQYIVGRSRKQNNPLLIHVDTKAGHGAGKPTAKVIEEVSDMFAFI
ARCLNIDWIP
3D structure
PDB1h2y Electrostatic Effects and Binding Determinants in the Catalysis of Prolyl Oligopeptidase: Site Specific Mutagenesis at the Oxyanion Binding Site
ChainA
Resolution1.78 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) F473 S554 D641 H680
Catalytic site (residue number reindexed from 1) F473 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 ZPR A M235 F473 F476 S554 N555 A594 W595 R643 V644 M235 F473 F476 S554 N555 A594 W595 R643 V644 BindingDB: IC50=0.33nM
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1h2y, PDBe:1h2y, PDBj:1h2y
PDBsum1h2y
PubMed12202494
UniProtP23687|PPCE_PIG Prolyl endopeptidase (Gene Name=PREP)

[Back to BioLiP]