Structure of PDB 3ago Chain A

Receptor sequence
>3agoA (length=114) Species: 5271 (Ustilago sphaerogena) [Search protein sequence]
CDIPQSTNCGGNVYSNDDINTAIQGALDDVANGDRPDNYPHQYYDEASED
ITLCCGSGPWSEFPLVYNGPYYSSRDNYVSPGPDRVIYQTNTGEFCATVT
HTGAASYDGFTQCS
3D structure
PDB3ago Isomerization mechanism of aspartate to isoaspartate implied by structures of Ustilago sphaerogena ribonuclease U2 complexed with adenosine 3'-monophosphate
ChainA
Resolution0.99 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) Y39 H41 E62 R85 H101 F110
Catalytic site (residue number reindexed from 1) Y39 H41 E62 R85 H101 F110
Enzyme Commision number 4.6.1.20: ribonuclease U2.
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 3AM A Y39 H41 Y44 E46 E49 E62 R85 H101 D108 F110 Y39 H41 Y44 E46 E49 E62 R85 H101 D108 F110
BS02 CA A D29 A31 Y39 D29 A31 Y39
BS03 CA A D45 I51 D45 I51
Gene Ontology
Molecular Function
GO:0003723 RNA binding
GO:0004519 endonuclease activity
GO:0004521 RNA endonuclease activity
GO:0004540 RNA nuclease activity
GO:0016829 lyase activity
GO:0033899 ribonuclease U2 activity
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:3ago, PDBe:3ago, PDBj:3ago
PDBsum3ago
PubMed20606265
UniProtP00654|RNU2_USTSP Ribonuclease U2 (Gene Name=RNU2)

[Back to BioLiP]