Structure of PDB 1epn Chain E

Receptor sequence
>1epnE (length=330) Species: 5116 (Cryphonectria parasitica) [Search protein sequence]
STGSATTTPIDSLDDAYITPVQIGTPAQTLNLDFDTGSSDLWVFSSETTA
SEVDGQTIYTPSKSTTAKLLSGATWSISYGDGSSSSGDVYTDTVSVGGLT
VTGQAVESAKKVSSSFTEDSTIDGLLGLAFSTLNTVSPTQQKTFFDNAKA
SLDSPVFTADLGYHAPGTYNFGFIDTTAYTGSITYTAVSTKQGFWEWTST
GYAVGSGTFKSTSIDGIADTGTTLLYLPATVVSAYWAQVSGAKSSSSVGG
YVFPCSATLPSFTFGVGSARIVIPGDYIDFGPISTGSSSCFGGIQSSAGI
GINIFGDVALKAAFVVFNGATTPTLGFASK
3D structure
PDB1epn A structural comparison of 21 inhibitor complexes of the aspartic proteinase from Endothia parasitica.
ChainE
Resolution1.6 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 2ZS E D12 A13 D30 D32 Y75 G76 D77 F111 L120 F189 D215 G217 T218 T219 D15 A16 D33 D35 Y79 G80 D81 F116 L125 F194 D219 G221 T222 T223
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:1epn, PDBe:1epn, PDBj:1epn
PDBsum1epn
PubMed7703859
UniProtP11838|CARP_CRYPA Endothiapepsin (Gene Name=EAPA)

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