Structure of PDB 2er6 Chain E

Receptor sequence
>2er6E (length=330) Species: 5116 (Cryphonectria parasitica) [Search protein sequence]
STGSATTTPIDSLDDAYITPVQIGTPAQTLNLDFDTGSSDLWVFSSETTA
SEVDGQTIYTPSKSTTAKLLSGATWSISYGDGSSSSGDVYTDTVSVGGLT
VTGQAVESAKKVSSSFTEDSTIDGLLGLAFSTLNTVSPTQQKTFFDNAKA
SLDSPVFTADLGYHAPGTYNFGFIDTTAYTGSITYTAVSTKQGFWEWTST
GYAVGSGTFKSTSIDGIADTGTTLLYLPATVVSAYWAQVSGAKSSSSVGG
YVFPCSATLPSFTFGVGSARIVIPGDYIDFGPISTGSSSCFGGIQSSAGI
GINIFGDVALKAAFVVFNGATTPTLGFASK
3D structure
PDB2er6 The structure of a synthetic pepsin inhibitor complexed with endothiapepsin
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 peptide E D30 D32 G34 I73 S74 Y75 G76 D77 F111 L120 L128 D215 G217 T218 T219 Y222 I297 I301 D33 D35 G37 I77 S78 Y79 G80 D81 F116 L125 L133 D219 G221 T222 T223 Y226 I300 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:2er6, PDBe:2er6, PDBj:2er6
PDBsum2er6
PubMed3119339
UniProtP11838|CARP_CRYPA Endothiapepsin (Gene Name=EAPA)

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