Structure of PDB 3prs Chain A

Receptor sequence
>3prsA (length=330) Species: 5116 (Cryphonectria parasitica) [Search protein sequence]
STGSATTTPIDSLDDAYITPVQIGTPAQTLNLDFDTGSSDLWVFSSETTA
SEVDGQTIYTPSKSTTAKLLSGATWSISYGDGSSSSGDVYTDTVSVGGLT
VTGQAVESAKKVSSSFTEDSTIDGLLGLAFSTLNTVSPTQQKTFFDNAKA
SLDSPVFTADLGYHAPGTYNFGFIDTTAYTGSITYTAVSTKQGFWEWTST
GYAVGSGTFKSTSIDGIADTGTTLLYLPATVVSAYWAQVSGAKSSSSVGG
YVFPCSATLPSFTFGVGSARIVIPGDYIDFGPISTGSSSCFGGIQSSAGI
GINIFGDVALKAAFVVFNGATTPTLGFASK
3D structure
PDB3prs Experimental and computational active site mapping as a starting point to fragment-based lead discovery.
ChainA
Resolution1.38 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D35 S38 D40 W42 Y79 D219 T222
Catalytic site (residue number reindexed from 1) D35 S38 D40 W42 Y79 D219 T222
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 RIT A D15 D33 D35 G37 S78 Y79 G80 D81 D119 F194 D219 G221 T222 T223 Y226 I304 D15 D33 D35 G37 S78 Y79 G80 D81 D119 F194 D219 G221 T222 T223 Y226 I304 PDBbind-CN: -logKd/Ki=7.82,Ki=15nM
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:3prs, PDBe:3prs, PDBj:3prs
PDBsum3prs
PubMed22213702
UniProtP11838|CARP_CRYPA Endothiapepsin (Gene Name=EAPA)

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