Structure of PDB 3bcn Chain A Binding Site BS01

Receptor Information
>3bcn Chain A (length=209) Species: 52861 (Tabernaemontana divaricata) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LPEHVDWRAKGAVIPLKNQGKCGSCWAFSTVTTVESINQIRTGNLISLSE
QQLVDCSKKNHGCKGGYFDRAYQYIIANGGIDTEANYPYKAFQGPCRAAK
KVVRIDGCKGVPQCNENALKNAVASQPSVVAIDASSKQFQHYKGGIFTGP
CGTKLNHGVVIVGYGKDYWIVRNSWGRHWGEQGYTRMKRVGGCGLCGIAR
LPFYPTKAA
Ligand information
Ligand IDE64
InChIInChI=1S/C15H29N5O5/c1-9(2)7-10(20-14(25)11(21)8-12(22)23)13(24)18-5-3-4-6-19-15(16)17/h9-11,21H,3-8H2,1-2H3,(H,18,24)(H,20,25)(H,22,23)(H4,16,17,19)/p+1/t10-,11-/m0/s1
InChIKeyQPQNJAXBPHVASB-QWRGUYRKSA-O
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC(C)C[C@@H](C(=O)NCCCCNC(=[NH2+])N)NC(=O)[C@H](CC(=O)O)O
OpenEye OEToolkits 1.5.0CC(C)CC(C(=O)NCCCCNC(=[NH2+])N)NC(=O)C(CC(=O)O)O
CACTVS 3.341CC(C)C[C@H](NC(=O)[C@@H](O)CC(O)=O)C(=O)NCCCCNC(N)=[NH2+]
CACTVS 3.341CC(C)C[CH](NC(=O)[CH](O)CC(O)=O)C(=O)NCCCCNC(N)=[NH2+]
ACDLabs 10.04O=C(O)CC(O)C(=O)NC(C(=O)NCCCCNC(=[NH2+])\N)CC(C)C
FormulaC15 H30 N5 O5
NameN-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE
ChEMBL
DrugBankDB04276
ZINC
PDB chain3bcn Chain A Residue 214 [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]
PDB3bcn Structural insights into the substrate specificity and activity of ervatamins, the papain-like cysteine proteases from a tropical plant, Ervatamia coronaria
Resolution2.85 Å
Binding residue
(original residue number in PDB)		G23 C25 W26 G65 G66 N156 H157
Binding residue
(residue number reindexed from 1)		G23 C25 W26 G65 G66 N156 H157
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=7.12,IC50=76.25nM
Enzymatic activity
Catalytic site (original residue number in PDB) Q19 C25 H157 N173
Catalytic site (residue number reindexed from 1) Q19 C25 H157 N173
Enzyme Commision number 3.4.22.-
Gene Ontology
Molecular Function
GO:0004197 cysteine-type endopeptidase activity
GO:0008234 cysteine-type peptidase activity
Biological Process
GO:0006508 proteolysis
GO:0051603 proteolysis involved in protein catabolic process
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005764 lysosome

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3bcn, PDBe:3bcn, PDBj:3bcn
PDBsum3bcn
PubMed18167146
UniProtA5YVK8|ERVA_TABDI Ervatamin-A (Fragment)

[Back to BioLiP]