Structure of PDB 5qbh Chain A Binding Site BS01

Receptor Information
>5qbh Chain A (length=330) Species: 5116 (Cryphonectria parasitica) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
STGSATTTPIDSLDDAYITPVQIGTPAQTLNLDFDTGSSDLWVFSSETTA
SEVDGQTIYTPSKSTTAKLLSGATWSISYGDGSSSSGDVYTDTVSVGGLT
VTGQAVESAKKVSSSFTEDSTIDGLLGLAFSTLNTVSPTQQKTFFDNAKA
SLDSPVFTADLGYHAPGTYNFGFIDTTAYTGSITYTAVSTKQGFWEWTST
GYAVGSGTFKSTSIDGIADTGTTLLYLPATVVSAYWAQVSGAKSSSSVGG
YVFPCSATLPSFTFGVGSARIVIPGDYIDFGPISTGSSSCFGGIQSSAGI
GINIFGDVALKAAFVVFNGATTPTLGFASK
Ligand information
Ligand IDD8M
InChIInChI=1S/C13H19N3O4/c14-6-10-13(19)12(18)9(20-10)5-11(17)16-7-8-3-1-2-4-15-8/h1-4,9-10,12-13,18-19H,5-7,14H2,(H,16,17)/t9-,10+,12-,13+/m0/s1
InChIKeyBIGFPMOCLWRIMB-JULQROHOSA-N
SMILES
SoftwareSMILES
CACTVS 3.385NC[CH]1O[CH](CC(=O)NCc2ccccn2)[CH](O)[CH]1O
CACTVS 3.385NC[C@H]1O[C@@H](CC(=O)NCc2ccccn2)[C@H](O)[C@@H]1O
OpenEye OEToolkits 2.0.6c1ccnc(c1)CNC(=O)CC2C(C(C(O2)CN)O)O
OpenEye OEToolkits 2.0.6c1ccnc(c1)CNC(=O)C[C@H]2[C@@H]([C@@H]([C@H](O2)CN)O)O
ACDLabs 12.01OC2C(CC(=O)NCc1ccccn1)OC(C2O)CN
FormulaC13 H19 N3 O4
Name2-[(2S,3R,4S,5R)-5-(aminomethyl)-3,4-dihydroxytetrahydrofuran-2-yl]-N-(pyridin-2-ylmethyl)acetamide
ChEMBL
DrugBank
ZINCZINC000225394883
PDB chain5qbh Chain A Residue 404 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB5qbh Crystal structure of Endothiapepsin
Resolution1.469 Å
Binding residue
(original residue number in PDB)		G37 Y79 G80 D81 L125 F194 D219 G221 T222
Binding residue
(residue number reindexed from 1)		G37 Y79 G80 D81 L125 F194 D219 G221 T222
Annotation score1
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.
Gene Ontology
Molecular Function
GO:0004190 aspartic-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5qbh, PDBe:5qbh, PDBj:5qbh
PDBsum5qbh
PubMed
UniProtP11838|CARP_CRYPA Endothiapepsin (Gene Name=EAPA)

[Back to BioLiP]