Structure of PDB 3fqj Chain A

Receptor sequence
>3fqjA (length=353) Species: 10090 (Mus musculus) [Search protein sequence]
PSLRTQPSLYSGPFPFYRRPSELGCFSLDAQRQYHGDARALRYYSPPPIN
GPGPDFDLRDGYPDRYQPRDEEVQERLDHLLRWVLEHRNQGWLAGATVTW
RGHLTKLLTTPYERQEGWQLAASRFQGTLYLSEVETPAARAQRLARPPLL
RELMYMGYKFEQYMCADKPGGSPDPSGEVNTNVAYCSVLRSRLGNHPLLF
SGEVDCLNPQAPCTQPPSCYVELKTSKEMHSPGQWRSFYRHKLLKWWAQS
FLPGVPHVVAGFRNPEGFVCSLKTFPTMEMFENVRNDREGWNPSVCMNFC
AAFLSFAQSTVVQDDPRLVHLFSWEPGGPVTVSVHRDAPYAFLPSWYVET
MTQ
3D structure
PDB3fqj Structure and function of the 5'-->3' exoribonuclease Rat1 and its activating partner Rai1.
ChainA
Resolution2.623 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.1.13.-
3.6.1.-
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 MG A D236 E253 K255 D205 E222 K224
BS02 GDP A R58 R95 E101 W131 R132 G133 C217 G233 E234 Q280 R32 R69 E75 W100 R101 G102 C186 G202 E203 Q249
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0000287 magnesium ion binding
GO:0003723 RNA binding
GO:0003729 mRNA binding
GO:0004527 exonuclease activity
GO:0008409 5'-3' exonuclease activity
GO:0034353 mRNA 5'-diphosphatase activity
GO:0046872 metal ion binding
GO:0110152 RNA NAD+-cap (NAD+-forming) hydrolase activity
Biological Process
GO:0006402 mRNA catabolic process
GO:0050779 RNA destabilization
GO:0071028 nuclear mRNA surveillance
GO:0090304 nucleic acid metabolic process
GO:0110155 NAD-cap decapping
Cellular Component
GO:0005634 nucleus

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3fqj, PDBe:3fqj, PDBj:3fqj
PDBsum3fqj
PubMed19194460
UniProtO70348|DXO_MOUSE Decapping and exoribonuclease protein (Gene Name=Dxo)

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