Structure of PDB 3le7 Chain A

Receptor sequence
>3le7A (length=261) Species: 29725 (Phytolacca dioica) [Search protein sequence]
INTITYDAGNTTINKYATFMESLRNEAKDPSLQCYGIPMLPNNSSTIKYL
LVKLQGASQKTITLMLRRNNLYVMGYSDPFNGNCRYHIFNDITGTERTNV
ENTLCSSSSSRDAKPINYNSLYSTLEKKAEVNSRSQVQLGIQILSSDIGK
ISGQSSFTDKTEAKFLLVAIQMVSEAARFKYIENQVKTNFNRDFSPNDKI
LDLEENWGKISTAIHDATNGALPKPLELKNADGTKWIVLRVDEIKPDMGL
LNYVNGTCQTT
3D structure
PDB3le7 The role of the glycan moiety on the structure-function relationships of PD-L1, type 1 ribosome-inactivating protein from P. dioica leaves
ChainA
Resolution1.65 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) V76 E178 R181
Catalytic site (residue number reindexed from 1) V73 E175 R178
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 Y75 V76 S123 Y125 I173 S177 R181 Y72 V73 S120 Y122 I170 S174 R178
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3le7, PDBe:3le7, PDBj:3le7
PDBsum3le7
PubMed20174685
UniProtP84853|RIPL1_PHYDI Ribosome-inactivating protein PD-L1/PD-L2

[Back to BioLiP]