Structure of PDB 4q2v Chain A

Receptor sequence
>4q2vA (length=259) Species: 3988 (Ricinus communis) [Search protein sequence]
QYPIINFTTAGATVQSYTNFIRAVRGRLTTGADVRHEIPVLPNRVGLPIN
QRFILVELSNHAELSVTLALDVTNAYVVGYRAGNSAYFFHPDNQEDAEAI
THLFTDVQNRYTFAFGGNYDRLEQLAGNLRENIELGNGPLEEAISALYYY
STGGTQLPTLARSFIICIQMISEAARFQYIEGEMRTRIRYNRRSAPDPSV
ITLENSWGRLSTAIQESNQGAFASPIQLQRRNGSKFSVYDVSILIPIIAL
MVYRCAPPP
3D structure
PDB4q2v Baicalin inhibits the lethality of ricin in mice by inducing protein oligomerization.
ChainA
Resolution2.198 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) V77 E173 R176
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 0XE A R213 E220 R258 C259 R209 E216 R254 C255
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:4q2v, PDBe:4q2v, PDBj:4q2v
PDBsum4q2v
PubMed25847243
UniProtP02879|RICI_RICCO Ricin

[Back to BioLiP]