Structure of PDB 1aha Chain A

Receptor sequence
>1ahaA (length=246) Species: 3673 (Momordica charantia) [Search protein sequence]
DVSFRLSGADPRSYGMFIKDLRNALPFREKVYNIPLLLPSVSGAGRYLLM
HLFNYDGKTITVAVDVTNVYIMGYLADTTSYFFNEPAAELASQYVFRDAR
RKITLPYSGNYERLQIAAGKPREKIPIGLPALDSAISTLLHYDSTAAAGA
LLVLIQTTAEAARFKYIEQQIQERAYRDEVPSLATISLENSWSGLSKQIQ
LAQGNNGIFRTPIVLVDNKGNRVQITNVTSKVVTSNIQLLLNTRNI
3D structure
PDB1aha The N-glycosidase mechanism of ribosome-inactivating proteins implied by crystal structures of alpha-momorcharin.
ChainA
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 ADE A Y70 I71 G109 Y111 I155 R163 Y70 I71 G109 Y111 I155 R163
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

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Molecular Function
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Biological Process
External links
PDB RCSB:1aha, PDBe:1aha, PDBj:1aha
PDBsum1aha
PubMed8075985
UniProtP16094|RIP1_MOMCH Ribosome-inactivating protein momordin I

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