Structure of PDB 1gvx Chain A Binding Site BS01

Receptor Information
>1gvx Chain A (length=328) Species: 5116 (Cryphonectria parasitica) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
STGSATTTPIDSLDDAYITPVQIGTPAQTLNLDFDTGSSDLWVFSSETTA
SEVQTIYTPSKSTTAKLLSGATWSISYGDGSSSSGDVYTDTVSVGGLTVT
GQAVESAKKVSSSFTEDSTIDGLLGLAFSTLNTVSPTQQKTFFDNAKASL
DSPVFTADLGYHAPGTYNFGFIDTTAYTGSITYTAVSTKQGFWEWTSTGY
AVGSGTFKSTSIDGIADTGTTLLYLPATVVSAYWAQVSGAKSSSSVGGYV
FPCSATLPSFTFGVGSARIVIPGDYIDFGPISTGSSSCFGGIQSSAGIGI
NIFGDVALKAAFVVFNGATTPTLGFASK
Ligand information
Receptor-Ligand Complex Structure
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PDB1gvx Five Atomic Resolution Structures of Endothiapepsin Inhibitor Complexes: Implications for the Aspartic Proteinase Mechanism
Resolution1.0 Å
Binding residue
(original residue number in PDB)		D15 D33 D35 G37 S78 Y79 G80 D81 F116 L133 T135 D219 G221 T222 T223 I304
Binding residue
(residue number reindexed from 1)		D15 D33 D35 G37 S76 Y77 G78 D79 F114 L131 T133 D217 G219 T220 T221 I302
Enzymatic activity
Catalytic site (original residue number in PDB) D35 S38 D40 W42 G80 T220 T223
Catalytic site (residue number reindexed from 1) D35 S38 D40 W42 G78 T218 T221
Enzyme Commision number 3.4.23.22: endothiapepsin.
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:1gvx, PDBe:1gvx, PDBj:1gvx
PDBsum1gvx
PubMed12083527
UniProtP11838|CARP_CRYPA Endothiapepsin (Gene Name=EAPA)

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