Structure of PDB 5er2 Chain E

Receptor sequence
>5er2E (length=330) Species: 5116 (Cryphonectria parasitica) [Search protein sequence]
STGSATTTPIDSLDDAYITPVQIGTPAQTLNLDFDTGSSDLWVFSSETTA
SEVDGQTIYTPSKSTTAKLLSGATWSISYGDGSSSSGDVYTDTVSVGGLT
VTGQAVESAKKVSSSFTEDSTIDGLLGLAFSTLNTVSPTQQKTFFDNAKA
SLDSPVFTADLGYHAPGTYNFGFIDTTAYTGSITYTAVSTKQGFWEWTST
GYAVGSGTFKSTSIDGIADTGTTLLYLPATVVSAYWAQVSGAKSSSSVGG
YVFPCSATLPSFTFGVGSARIVIPGDYIDFGPISTGSSSCFGGIQSSAGI
GINIFGDVALKAAFVVFNGATTPTLGFASK
3D structure
PDB5er2 High-resolution X-ray diffraction study of the complex between endothiapepsin and an oligopeptide inhibitor: the analysis of the inhibitor binding and description of the rigid body shift in the enzyme.
ChainE
Resolution1.8 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 0EK E D30 D32 G34 Y75 G76 D77 D114 L128 F189 I213 D215 G217 T218 T219 I297 I301 D33 D35 G37 Y79 G80 D81 D119 L133 F194 I217 D219 G221 T222 T223 I300 I304 MOAD: Ki=0.27uM
PDBbind-CN: -logKd/Ki=6.57,Ki=0.27uM
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:5er2, PDBe:5er2, PDBj:5er2
PDBsum5er2
PubMed2676515
UniProtP11838|CARP_CRYPA Endothiapepsin (Gene Name=EAPA)

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