Structure of PDB 4s2r Chain Q

Receptor sequence
>4s2rQ (length=612) Species: 6239 (Caenorhabditis elegans) [Search protein sequence]
MTALEKLAKLRSLFHSERVLALTSSKPMVAYLLPSTDAHHSEYLADYDFR
VKFLSGFSGSNAYVVVTDREALLWTDGRYFTQAGNQLDSNSWKLMKQGQP
DSITVVDWLVRELERGSVIGFDPTLSTFDAGSKTFKRLKAAGLQPVSIPG
NLVDEFWTDRPRLAGEPVVVLDVEDTGLTTSKKVENLREKLKQKKCDAAV
FTLLDDVMWLLNIRGSDIPYNPLAYSYLFVAMREIHVFIDNEKLDEKSRA
HFHKSNVSIHPYGEVYSWISNWLKAKEASKEPHMVYLTPETNYAIGSIIG
EENSMVDTSLVQTAKATKNDHEMQGMRNSHLRDSAALVEFLCWLEKELLS
GKRYTEIELADKIDHLRSLQDKYVTLSFDTISAVGDHAALPHYKPLGESG
NRKAAANQVFLLDSGAHYGDGTTDVTRTVWYTNPPKEFILHNTLVLKGHI
NLARAKFPDGIYGSRLDTLTRDALWKLGLDFEHGTGHGVGHYLNVHEGPI
GIGHTGGELHASQVLTIEPGFYAKEKYGIRIENCYETVEAVVMSKAQNFL
TFKSLTLVPIQTSIVDKSLLIEEEINWLNQYHARVLKEVGEHLQKRGKTD
ELKWLAEACKPI
3D structure
PDB4s2r Crystal structure of X-prolyl aminopeptidase from Caenorhabditis elegans: A cytosolic enzyme with a di-nuclear active site.
ChainQ
Resolution1.949 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.4.11.9: Xaa-Pro aminopeptidase.
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 ZN Q D413 D424 E536 D413 D424 E532
BS02 ZN Q D424 H487 E522 E536 D424 H487 E518 E532
Gene Ontology
Molecular Function
GO:0004177 aminopeptidase activity
GO:0008270 zinc ion binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0070006 metalloaminopeptidase activity
Biological Process
GO:0006508 proteolysis
GO:0051603 proteolysis involved in protein catabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4s2r, PDBe:4s2r, PDBj:4s2r
PDBsum4s2r
PubMed25905034
UniProtO44750|XPP_CAEEL Xaa-Pro aminopeptidase app-1 (Gene Name=app-1)

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