Structure of PDB 1oex Chain A

Receptor sequence
>1oexA (length=328) Species: 5116 (Cryphonectria parasitica) [Search protein sequence]
STGSATTTPIDSLDDAYITPVQIGTPAQTLNLDFDTGSSDLWVFSSETTA
SEVQTIYTPSKSTTAKLLSGATWSISYGDGSSSSGDVYTDTVSVGGLTVT
GQAVESAKKVSSSFTEDSTIDGLLGLAFSTLNTVSPTQQKTFFDNAKASL
DSPVFTADLGYHAPGTYNFGFIDTTAYTGSITYTAVSTKQGFWEWTSTGY
AVGSGTFKSTSIDGIADTGTTLLYLPATVVSAYWAQVSGAKSSSSVGGYV
FPCSATLPSFTFGVGSARIVIPGDYIDFGPISTGSSSCFGGIQSSAGIGI
NIFGDVALKAAFVVFNGATTPTLGFASK
3D structure
PDB1oex Atomic Resolution Analysis of the Catalytic Site of an Aspartic Proteinase and an Unexpected Mode of Binding by Short Peptides
ChainA
Resolution1.1 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 G79 T219 T222
Catalytic site (residue number reindexed from 1) D35 S38 D40 W42 G78 T218 T221
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 A L13 D15 D35 G37 I76 S77 Y78 G79 D80 I121 L132 F193 D218 G220 T221 T222 F279 G280 P281 L13 D15 D35 G37 I75 S76 Y77 G78 D79 I120 L131 F192 D217 G219 T220 T221 F278 G279 P280
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:1oex, PDBe:1oex, PDBj:1oex
PDBsum1oex
PubMed12876323
UniProtP11838|CARP_CRYPA Endothiapepsin (Gene Name=EAPA)

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