Structure of PDB 2er9 Chain E

Receptor sequence
>2er9E (length=330) Species: 5116 (Cryphonectria parasitica) [Search protein sequence]
STGSATTTPIDSLDDAYITPVQIGTPAQTLNLDFDTGSSDLWVFSSETTA
SEVDGQTIYTPSKSTTAKLLSGATWSISYGDGSSSSGDVYTDTVSVGGLT
VTGQAVESAKKVSSSFTEDSTIDGLLGLAFSTLNTVSPTQQKTFFDNAKA
SLDSPVFTADLGYHAPGTYNFGFIDTTAYTGSITYTAVSTKQGFWEWTST
GYAVGSGTFKSTSIDGIADTGTTLLYLPATVVSAYWAQVSGAKSSSSVGG
YVFPCSATLPSFTFGVGSARIVIPGDYIDFGPISTGSSSCFGGIQSSAGI
GINIFGDVALKAAFVVFNGATTPTLGFASK
3D structure
PDB2er9 X-ray studies of aspartic proteinase-statine inhibitor complexes.
ChainE
Resolution2.2 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 peptide E D12 D32 Y75 G76 D77 D114 D215 G217 T218 T219 I301 D15 D35 Y79 G80 D81 D119 D219 G221 T222 T223 I304
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:2er9, PDBe:2er9, PDBj:2er9
PDBsum2er9
PubMed2690945
UniProtP11838|CARP_CRYPA Endothiapepsin (Gene Name=EAPA)

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