Structure of PDB 1il5 Chain A

Receptor sequence
>1il5A (length=264) Species: 3988 (Ricinus communis) [Search protein sequence]
IFPKQYPIINFTTAGATVQSYTNFIRAVRGRLTTGADVHEIPVLPNRVGL
PINQRFILVELSNHAELSVTLALDVTNAYVVGYRAGNSAYFFHPDNQEDA
EAITHLFTDVQNRYTFAFGGNYDRLEQLAGNLRENIELGNGPLEEAISAL
YYYSTGGTQLPTLARSFIICIQMISEAARFQYIEGEMRTRIRYNRRSAPD
PSVITLENSWGRLSTAIQESNQGAFASPIQLQRRNGSKFSVYDVSILIPI
IALMVYRCAPPPQF
3D structure
PDB1il5 Structure-based design and characterization of novel platforms for ricin and shiga toxin inhibition.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) V81 E177 R180
Catalytic site (residue number reindexed from 1) V80 E176 R179
Enzyme Commision number 3.2.2.22: rRNA N-glycosylase.
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 DDP A Y80 N122 Y123 R180 Y79 N121 Y122 R179 PDBbind-CN: -logKd/Ki=2.66,IC50=2.2mM
Gene Ontology
Molecular Function
GO:0030598 rRNA N-glycosylase activity
Biological Process
GO:0017148 negative regulation of translation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1il5, PDBe:1il5, PDBj:1il5
PDBsum1il5
PubMed11754581
UniProtP02879|RICI_RICCO Ricin

[Back to BioLiP]