Structure of PDB 3t6i Chain A

Receptor sequence
>3t6iA (length=330) Species: 5116 (Cryphonectria parasitica) [Search protein sequence]
STGSATTTPIDSLDDAYITPVQIGTPAQTLNLDFDTGSSDLWVFSSETTA
SEVDGQTIYTPSKSTTAKLLSGATWSISYGDGSSSSGDVYTDTVSVGGLT
VTGQAVESAKKVSSSFTEDSTIDGLLGLAFSTLNTVSPTQQKTFFDNAKA
SLDSPVFTADLGYHAPGTYNFGFIDTTAYTGSITYTAVSTKQGFWEWTST
GYAVGSGTFKSTSIDGIADTGTTLLYLPATVVSAYWAQVSGAKSSSSVGG
YVFPCSATLPSFTFGVGSARIVIPGDYIDFGPISTGSSSCFGGIQSSAGI
GINIFGDVALKAAFVVFNGATTPTLGFASK
3D structure
PDB3t6i Endothiapepsin in complex with an azepin derivative
ChainA
Resolution1.32 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 NC8 A D35 G37 I77 S78 Y79 G80 F194 D219 G221 T222 Y226 I300 D35 G37 I77 S78 Y79 G80 F194 D219 G221 T222 Y226 I300
BS02 NC9 A I10 D15 Y79 D81 G221 T222 T223 Y226 I10 D15 Y79 D81 G221 T222 T223 Y226
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:3t6i, PDBe:3t6i, PDBj:3t6i
PDBsum3t6i
PubMed
UniProtP11838|CARP_CRYPA Endothiapepsin (Gene Name=EAPA)

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