Structure of PDB 5er1 Chain E

Receptor sequence
>5er1E (length=330) Species: 5116 (Cryphonectria parasitica) [Search protein sequence]
STGSATTTPIDSLDDAYITPVQIGTPAQTLNLDFDTGSSDLWVFSSETTA
SEVDGQTIYTPSKSTTAKLLSGATWSISYGDGSSSSGDVYTDTVSVGGLT
VTGQAVESAKKVSSSFTEDSTIDGLLGLAFSTLNTVSPTQQKTFFDNAKA
SLDSPVFTADLGYHAPGTYNFGFIDTTAYTGSITYTAVSTKQGFWEWTST
GYAVGSGTFKSTSIDGIADTGTTLLYLPATVVSAYWAQVSGAKSSSSVGG
YVFPCSATLPSFTFGVGSARIVIPGDYIDFGPISTGSSSCFGGIQSSAGI
GINIFGDVALKAAFVVFNGATTPTLGFASK
3D structure
PDB5er1 X-Ray Analysis and Circular Dichroism of the Acid Protease from Endothia Parasitica and Chymosin
ChainE
Resolution2.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.4.23.22: endothiapepsin.
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 0HT E D32 G34 S74 Y75 G76 D77 L128 F189 D215 G217 D35 G37 S78 Y79 G80 D81 L133 F194 D219 G221 MOAD: Ki=960nM
PDBbind-CN: -logKd/Ki=6.02,Ki=960nM
Gene Ontology
Molecular Function
GO:0004190 aspartic-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:5er1, PDBe:5er1, PDBj:5er1
PDBsum5er1
PubMed
UniProtP11838|CARP_CRYPA Endothiapepsin (Gene Name=EAPA)

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