Structure of PDB 4er1 Chain E

Receptor sequence
>4er1E (length=330) Species: 5116 (Cryphonectria parasitica) [Search protein sequence]
STGSATTTPIDSLDDAYITPVQIGTPAQTLNLDFDTGSSDLWVFSSETTA
SEVDGQTIYTPSKSTTAKLLSGATWSISYGDGSSSSGDVYTDTVSVGGLT
VTGQAVESAKKVSSSFTEDSTIDGLLGLAFSTLNTVSPTQQKTFFDNAKA
SLDSPVFTADLGYHAPGTYNFGFIDTTAYTGSITYTAVSTKQGFWEWTST
GYAVGSGTFKSTSIDGIADTGTTLLYLPATVVSAYWAQVSGAKSSSSVGG
YVFPCSATLPSFTFGVGSARIVIPGDYIDFGPISTGSSSCFGGIQSSAGI
GINIFGDVALKAAFVVFNGATTPTLGFASK
3D structure
PDB4er1 The active site of aspartic proteinases
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 0ZP E D12 A13 D30 D32 G34 Y75 G76 D77 F189 I213 D215 G217 T218 T219 L220 Y222 I299 D15 A16 D33 D35 G37 Y79 G80 D81 F194 I217 D219 G221 T222 T223 L224 Y226 I302 MOAD: Ki=0.24uM
PDBbind-CN: -logKd/Ki=6.62,Ki=0.242uM
Gene Ontology
Molecular Function
GO:0004190 aspartic-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:4er1, PDBe:4er1, PDBj:4er1
PDBsum4er1
PubMed6381096
UniProtP11838|CARP_CRYPA Endothiapepsin (Gene Name=EAPA)

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