Structure of PDB 4q2v Chain A Binding Site BS01

Receptor Information
>4q2v Chain A (length=259) Species: 3988 (Ricinus communis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QYPIINFTTAGATVQSYTNFIRAVRGRLTTGADVRHEIPVLPNRVGLPIN
QRFILVELSNHAELSVTLALDVTNAYVVGYRAGNSAYFFHPDNQEDAEAI
THLFTDVQNRYTFAFGGNYDRLEQLAGNLRENIELGNGPLEEAISALYYY
STGGTQLPTLARSFIICIQMISEAARFQYIEGEMRTRIRYNRRSAPDPSV
ITLENSWGRLSTAIQESNQGAFASPIQLQRRNGSKFSVYDVSILIPIIAL
MVYRCAPPP
Ligand information
Ligand ID0XE
InChIInChI=1S/C21H18O11/c22-9-6-10(8-4-2-1-3-5-8)30-11-7-12(14(23)15(24)13(9)11)31-21-18(27)16(25)17(26)19(32-21)20(28)29/h1-7,16-19,21,23-27H,(H,28,29)/t16-,17-,18+,19-,21+/m0/s1
InChIKeyIKIIZLYTISPENI-ZFORQUDYSA-N
SMILES
SoftwareSMILES
CACTVS 3.370O[CH]1[CH](O)[CH](O[CH]([CH]1O)C(O)=O)Oc2cc3OC(=CC(=O)c3c(O)c2O)c4ccccc4
ACDLabs 12.01O=C(O)C4OC(Oc3c(O)c(O)c2c(OC(c1ccccc1)=CC2=O)c3)C(O)C(O)C4O
OpenEye OEToolkits 1.7.6c1ccc(cc1)C2=CC(=O)c3c(cc(c(c3O)O)O[C@H]4[C@@H]([C@H]([C@@H]([C@H](O4)C(=O)O)O)O)O)O2
CACTVS 3.370O[C@@H]1[C@@H](O)[C@@H](O[C@@H]([C@H]1O)C(O)=O)Oc2cc3OC(=CC(=O)c3c(O)c2O)c4ccccc4
OpenEye OEToolkits 1.7.6c1ccc(cc1)C2=CC(=O)c3c(cc(c(c3O)O)OC4C(C(C(C(O4)C(=O)O)O)O)O)O2
FormulaC21 H18 O11
Name5,6-dihydroxy-4-oxo-2-phenyl-4H-chromen-7-yl beta-D-glucopyranosiduronic acid;
Baicalin
ChEMBLCHEMBL485818
DrugBank
ZINCZINC000003943903
PDB chain4q2v Chain A Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4q2v Baicalin inhibits the lethality of ricin in mice by inducing protein oligomerization.
Resolution2.198 Å
Binding residue
(original residue number in PDB)		R213 E220 R258 C259
Binding residue
(residue number reindexed from 1)		R209 E216 R254 C255
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) V81 E177 R180
Catalytic site (residue number reindexed from 1) V77 E173 R176
Enzyme Commision number 3.2.2.22: rRNA N-glycosylase.
Gene Ontology
Molecular Function
GO:0030598 rRNA N-glycosylase activity
Biological Process
GO:0017148 negative regulation of translation

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Molecular Function
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Biological Process
External links
PDB RCSB:4q2v, PDBe:4q2v, PDBj:4q2v
PDBsum4q2v
PubMed25847243
UniProtP02879|RICI_RICCO Ricin

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