Structure of PDB 4y4j Chain A

Receptor sequence
>4y4jA (length=330) Species: 5116 (Cryphonectria parasitica) [Search protein sequence]
STGSATTTPIDSLDDAYITPVQIGTPAQTLNLDFDTGSSDLWVFSSETTA
SEVDGQTIYTPSKSTTAKLLSGATWSISYGDGSSSSGDVYTDTVSVGGLT
VTGQAVESAKKVSSSFTEDSTIDGLLGLAFSTLNTVSPTQQKTFFDNAKA
SLDSPVFTADLGYHAPGTYNFGFIDTTAYTGSITYTAVSTKQGFWEWTST
GYAVGSGTFKSTSIDGIADTGTTLLYLPATVVSAYWAQVSGAKSSSSVGG
YVFPCSATLPSFTFGVGSARIVIPGDYIDFGPISTGSSSCFGGIQSSAGI
GINIFGDVALKAAFVVFNGATTPTLGFASK
3D structure
PDB4y4j Structures of endothiapepsin-fragment complexes from crystallographic fragment screening using a novel, diverse and affordable 96-compound fragment library.
ChainA
Resolution1.03 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 LNR A D35 Y79 D81 S83 F116 G221 D35 Y79 D81 S83 F116 G221 MOAD: Kd=3.4mM
PDBbind-CN: -logKd/Ki=2.47,Kd=3.4mM
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:4y4j, PDBe:4y4j, PDBj:4y4j
PDBsum4y4j
PubMed27139825
UniProtP11838|CARP_CRYPA Endothiapepsin (Gene Name=EAPA)

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