Structure of PDB 2er7 Chain E

Receptor sequence
>2er7E (length=330) Species: 5116 (Cryphonectria parasitica) [Search protein sequence]
STGSATTTPIDSLDDAYITPVQIGTPAQTLNLDFDTGSSDLWVFSSETTA
SEVDGQTIYTPSKSTTAKLLSGATWSISYGDGSSSSGDVYTDTVSVGGLT
VTGQAVESAKKVSSSFTEDSTIDGLLGLAFSTLNTVSPTQQKTFFDNAKA
SLDSPVFTADLGYHAPGTYNFGFIDTTAYTGSITYTAVSTKQGFWEWTST
GYAVGSGTFKSTSIDGIADTGTTLLYLPATVVSAYWAQVSGAKSSSSVGG
YVFPCSATLPSFTFGVGSARIVIPGDYIDFGPISTGSSSCFGGIQSSAGI
GINIFGDVALKAAFVVFNGATTPTLGFASK
3D structure
PDB2er7 X-ray analyses of aspartic proteinases. III Three-dimensional structure of endothiapepsin complexed with a transition-state isostere inhibitor of renin at 1.6 A resolution.
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 peptide E I7 L10 D12 D32 G34 S74 Y75 G76 I117 L128 D215 G217 T218 T219 P277 I10 L13 D15 D35 G37 S78 Y79 G80 I122 L133 D219 G221 T222 T223 P282
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:2er7, PDBe:2er7, PDBj:2er7
PDBsum2er7
PubMed2266553
UniProtP11838|CARP_CRYPA Endothiapepsin (Gene Name=EAPA)

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