Structure of PDB 1nli Chain A

Receptor sequence
>1nliA (length=248) Species: 3677 (Trichosanthes kirilowii) [Search protein sequence]
MDVSFRLSGATSSSYGVFISNLRKALPNERKLYDIPLLRSSLPGSQRYAL
IHLTNYADETISVAIDVTNVYIMGYRAGDTSYFFNEASATEAAKYVFKDA
MRKVTLPYSGNYERLQTAAGKIRENIPLGLPALDSAITTLFYYNANSAAS
ALMVLIQSTSAAARYKFIEQQIGKRVDKTFLPSLAIISLANSWSALSKQI
QIASTNNGQFESPVVLINAQNQRVTITNVDAGVVTSNIALLLNRNNMA
3D structure
PDB1nli Structural basis for the interaction of [E160A-E189A]-trichosanthin with adenine.
ChainA
Resolution1.93 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) I71 A160 R163
Catalytic site (residue number reindexed from 1) I72 A161 R164
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 S159 R163 Y71 I72 G110 Y112 I156 S160 R164 MOAD: Kd=260uM
PDBbind-CN: -logKd/Ki=3.59,Kd=260uM
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
View graph for
Biological Process
External links
PDB RCSB:1nli, PDBe:1nli, PDBj:1nli
PDBsum1nli
PubMed12676436
UniProtP09989|RIPT_TRIKI Ribosome-inactivating protein alpha-trichosanthin

[Back to BioLiP]