Structure of PDB 5hct Chain A Binding Site BS01

Receptor Information
>5hct 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 ID61P
InChIInChI=1S/C30H30N8O2/c31-25(14-22-18-33-28-11-4-2-9-24(22)28)29(39)37-34-16-19-6-5-7-20(12-19)17-35-38-30(40)26(32)15-23-13-21-8-1-3-10-27(21)36-23/h1-13,16-18,25-26,33,36H,14-15,31-32H2,(H,37,39)(H,38,40)/b34-16+,35-17?/t25-,26?/m0/s1
InChIKeyZUYUCFMTHKDHJX-JQHDDIPESA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.4c1ccc2c(c1)cc([nH]2)CC(C(=O)NN=Cc3cccc(c3)C=NNC(=O)C(Cc4c[nH]c5c4cccc5)N)N
CACTVS 3.385NC(Cc1[nH]c2ccccc2c1)C(=O)N/N=C/c3cccc(\C=N\NC(=O)[C@@H](N)Cc4c[nH]c5ccccc45)c3
ACDLabs 12.01C(=N\NC(C(N)Cc1nc2c(c1)cccc2)=O)\c3cc(ccc3)[C@H]=NNC(=O)C(N)Cc4cnc5c4cccc5
CACTVS 3.385NC(Cc1[nH]c2ccccc2c1)C(=O)NN=Cc3cccc(C=NNC(=O)[CH](N)Cc4c[nH]c5ccccc45)c3
OpenEye OEToolkits 2.0.4c1ccc2c(c1)cc([nH]2)CC(C(=O)NN=Cc3cccc(c3)/C=N/NC(=O)[C@H](Cc4c[nH]c5c4cccc5)N)N
FormulaC30 H30 N8 O2
Name2-amino-N'-{3-[(E)-{2-[(2S)-2-amino-3-(1H-indol-3-yl)propanoyl]hydrazinylidene}methyl]benzylidene}-3-(1H-indol-2-yl)propanehydrazide (non-preferred name)
ChEMBL
DrugBank
ZINC
PDB chain5hct Chain A Residue 406 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5hct Fragment Linking and Optimization of Inhibitors of the Aspartic Protease Endothiapepsin: Fragment-Based Drug Design Facilitated by Dynamic Combinatorial Chemistry.
Resolution1.36 Å
Binding residue
(original residue number in PDB)		D33 D35 Y79 G80 D81 F116 D219 G221 T222 Y226 I300
Binding residue
(residue number reindexed from 1)		D33 D35 Y79 G80 D81 F116 D219 G221 T222 Y226 I300
Annotation score1
Binding affinityMOAD: Ki=0.0254uM
PDBbind-CN: -logKd/Ki=7.60,Ki=0.0254uM
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

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Molecular Function
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Biological Process
External links
PDB RCSB:5hct, PDBe:5hct, PDBj:5hct
PDBsum5hct
PubMed27400756
UniProtP11838|CARP_CRYPA Endothiapepsin (Gene Name=EAPA)

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