Structure of PDB 3n2d Chain A

Receptor sequence
>3n2dA (length=246) Species: 3672 (Momordica balsamina) [Search protein sequence]
DVSFRLSGADPSSYGMFIKDLRNALPHTEKVYNIPLLLPSVSGAGRYLLM
HLFNYDGNTITVAVDVTNVYIMGYLALTTSYFFNEPAADLASQYVFRSAR
RKITLPYSGNYERLQIAAGKPREKIPIGLPALDTAISTLLHYDSTAAAGA
LLVLIQTTAEAARFKYIEQQIQERAYRDEVPSSATISLENSWSGLSKQIQ
LAQGNNGVFRTPTVLVDSKGNRVQITNVTSNVVTSNIQLLLNTKNI
3D structure
PDB3n2d Crystal Structure of the Complex of type I Ribosome inactivating protein with hexapeptide Ser-Asp-Asp-Asp-Met-Gly at 2.2 A resolution
ChainA
Resolution2.22 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 A Y166 Q169 Q170 E173 R174 E179 V180 P181 S182 S218 N231 N236 Y166 Q169 Q170 E173 R174 E179 V180 P181 S182 S218 N231 N236
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016787 hydrolase activity
GO:0030598 rRNA N-glycosylase activity
GO:0090729 toxin activity
Biological Process
GO:0017148 negative regulation of translation
GO:0035821 modulation of process of another organism

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Molecular Function
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Biological Process
External links
PDB RCSB:3n2d, PDBe:3n2d, PDBj:3n2d
PDBsum3n2d
PubMed
UniProtD9J2T9

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