Structure of PDB 2jdl Chain B Binding Site BS01
Receptor Information
>2jdl Chain B (length=247) Species:
3677
(Trichosanthes kirilowii) [
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MVSFRLSGATSSSYGVFISNLRKALPNERKLYDIPLLRSSLPGSQRYALI
HLTNYADETISVAIDVTNVYIMGYRAGDTSYFFNEASATEAAKYVFKDAM
RKVTLPYSGNYERLQTAAGKIRENIPLGLPALDSAITTLFYYNANSAASA
LMVLIQSTSEAARYKFIEQQIGKRVDKTFLPSLAIISLENSWSALSKQIQ
IASTNNGQFESPVVLINAQNQRVTITNVDAGVVTSNIALLLNRNNMA
Ligand information
>2jdl Chain D (length=9) Species:
9606
(Homo sapiens) [
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DDMGFGLFD
Receptor-Ligand Complex Structure
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PDB
2jdl
The C-Terminal Fragment of the Ribosomal P Protein Complexed to Trichosanthin Reveals the Interaction between the Ribosome-Inactivating Protein and the Ribosome.
Resolution
2.2 Å
Binding residue
(original residue number in PDB)
F166 Q169 Q170 K173 R174 I216 A218 Q219 V223 I225 A230 G231 V232 S235 N236
Binding residue
(residue number reindexed from 1)
F166 Q169 Q170 K173 R174 I216 A218 Q219 V223 I225 A230 G231 V232 S235 N236
Enzymatic activity
Catalytic site (original residue number in PDB)
I71 E160 R163
Catalytic site (residue number reindexed from 1)
I71 E160 R163
Enzyme Commision number
3.2.2.22
: rRNA N-glycosylase.
Gene Ontology
Molecular Function
GO:0016787
hydrolase activity
GO:0030598
rRNA N-glycosylase activity
GO:0090729
toxin activity
Biological Process
GO:0006952
defense response
GO:0017148
negative regulation of translation
GO:0035821
modulation of process of another organism
GO:0050688
regulation of defense response to virus
View graph for
Molecular Function
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Biological Process
External links
PDB
RCSB:2jdl
,
PDBe:2jdl
,
PDBj:2jdl
PDBsum
2jdl
PubMed
19073700
UniProt
P09989
|RIPT_TRIKI Ribosome-inactivating protein alpha-trichosanthin
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