Structure of PDB 1gvx Chain A

Receptor sequence
>1gvxA (length=328) Species: 5116 (Cryphonectria parasitica) [Search protein sequence]
STGSATTTPIDSLDDAYITPVQIGTPAQTLNLDFDTGSSDLWVFSSETTA
SEVQTIYTPSKSTTAKLLSGATWSISYGDGSSSSGDVYTDTVSVGGLTVT
GQAVESAKKVSSSFTEDSTIDGLLGLAFSTLNTVSPTQQKTFFDNAKASL
DSPVFTADLGYHAPGTYNFGFIDTTAYTGSITYTAVSTKQGFWEWTSTGY
AVGSGTFKSTSIDGIADTGTTLLYLPATVVSAYWAQVSGAKSSSSVGGYV
FPCSATLPSFTFGVGSARIVIPGDYIDFGPISTGSSSCFGGIQSSAGIGI
NIFGDVALKAAFVVFNGATTPTLGFASK
3D structure
PDB1gvx Five Atomic Resolution Structures of Endothiapepsin Inhibitor Complexes: Implications for the Aspartic Proteinase Mechanism
ChainA
Resolution1.0 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 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.
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 D15 D33 D35 G37 S78 Y79 G80 D81 F116 L133 T135 D219 G221 T222 T223 I304 D15 D33 D35 G37 S76 Y77 G78 D79 F114 L131 T133 D217 G219 T220 T221 I302
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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