Structure of PDB 2jdl Chain B

Receptor sequence
>2jdlB (length=247) Species: 3677 (Trichosanthes kirilowii) [Search protein sequence]
MVSFRLSGATSSSYGVFISNLRKALPNERKLYDIPLLRSSLPGSQRYALI
HLTNYADETISVAIDVTNVYIMGYRAGDTSYFFNEASATEAAKYVFKDAM
RKVTLPYSGNYERLQTAAGKIRENIPLGLPALDSAITTLFYYNANSAASA
LMVLIQSTSEAARYKFIEQQIGKRVDKTFLPSLAIISLENSWSALSKQIQ
IASTNNGQFESPVVLINAQNQRVTITNVDAGVVTSNIALLLNRNNMA
3D structure
PDB2jdl The C-Terminal Fragment of the Ribosomal P Protein Complexed to Trichosanthin Reveals the Interaction between the Ribosome-Inactivating Protein and the Ribosome.
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 peptide B F166 Q169 Q170 K173 R174 I216 A218 Q219 V223 I225 A230 G231 V232 S235 N236 F166 Q169 Q170 K173 R174 I216 A218 Q219 V223 I225 A230 G231 V232 S235 N236
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

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Molecular Function
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Biological Process
External links
PDB RCSB:2jdl, PDBe:2jdl, PDBj:2jdl
PDBsum2jdl
PubMed19073700
UniProtP09989|RIPT_TRIKI Ribosome-inactivating protein alpha-trichosanthin

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