Structure of PDB 5vzj Chain K Binding Site BS02

Receptor Information
>5vzj Chain K (length=956) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PRRKRLADGLSVTQKVFVRSRNGGATKIVREHYLRSDIPCLSRSCTKCPQ
IVVPDAQNELPKFILSDSPLELSAPIGKHYVVLDTNVVLQAIDLLENPNC
FFDVIVPQIVLDEVRNKSYPVYTRLRTLCRDSDDHKRFIVFHNEFSEHTF
VERLPNETINDRNNRAIRKTCQWYSEHLKPYDINVVLVTNDRLNREAATK
EVESNIITKSLVQYIELLPNADDIRDSIPQMDFTFPEYYSTARVMGGLKN
GVLYQGNIQISEYNFLEGSVSLPRFSKPVLIVGQKNLNRAFNGDQVIVEL
LPQSEWKAPSSIVLDSEHFDVNDNPDIEAVISDKQRRLLAKDAMIAQRSK
KIQPTAKVVYIQRRSWRQYVGQLAPSSVDPQSSSTQNVFVILMDKCLPKV
RIRTRRAAELLDKRIVISIDSWPTTHKYPLGHFVRDLGTIESAQAETEAL
LLEHDVEYRPFSKKVLECLPAEGHDWKAPTKLDDPEAVSKDPLLTKRKDL
RDKLICSIDPPGCVDINDALHAKKLPNGNWEVGVHIADVTHFVKPGTALD
AEGAARGTSVYLVDKRIDMLPMLLGTDLCSLKPYVDRFAFSVIWELDDSA
NIVNVNFMKSVIRSREAFSYEQAQLRIDDKTQNDELTMGMRALLKLSVKL
KQKRLEAGALNLASPEVKVHMDDPNEVEIKKLLATNSLVEEFMLLANISV
ARKIYDAFPQTAMLRRHAAPPSTNFEILNEMLNTRKNMSISLESSKALAD
SLDRCVDPEDPYFNTLVRIMSTRCMMAAQYFYSGAYSYPDFRHYGLAVDI
YTHFTSPIRRYCDVVAHRQLAGAIGYEPLSLTHRDKNKMDMICRNINRKH
RNAQFAGRASIEYYVGQVMRNNESTETGYVIKVFNNGIVVLVPKFGVEGL
IRLDNLTEDPNSAAFDEVEYKLTFVPTNSDKPRDVYVFDKVEVQVRSVMD
AELLLK
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain5vzj Chain K Residue 2001 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB5vzj Structure and reconstitution of yeast Mpp6-nuclear exosome complexes reveals that Mpp6 stimulates RNA decay and recruits the Mtr4 helicase.
Resolution3.3 Å
Binding residue
(original residue number in PDB)		C47 C52 C55 H184
Binding residue
(residue number reindexed from 1)		C40 C45 C48 H177
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D543 D549 N551 D552 Y654 R847
Catalytic site (residue number reindexed from 1) D509 D515 N517 D518 Y620 R809
Enzyme Commision number 3.1.13.-
3.1.26.-
Gene Ontology
Molecular Function
GO:0000049 tRNA binding
GO:0000175 3'-5'-RNA exonuclease activity
GO:0003676 nucleic acid binding
GO:0003723 RNA binding
GO:0004519 endonuclease activity
GO:0004521 RNA endonuclease activity
GO:0004527 exonuclease activity
GO:0004540 RNA nuclease activity
GO:0005515 protein binding
Biological Process
GO:0000467 exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
GO:0006364 rRNA processing
GO:0006396 RNA processing
GO:0006397 mRNA processing
GO:0006401 RNA catabolic process
GO:0016075 rRNA catabolic process
GO:0043628 regulatory ncRNA 3'-end processing
GO:0070651 nonfunctional rRNA decay
GO:0071028 nuclear mRNA surveillance
GO:0071031 nuclear mRNA surveillance of mRNA 3'-end processing
GO:0071035 nuclear polyadenylation-dependent rRNA catabolic process
GO:0071038 TRAMP-dependent tRNA surveillance pathway
GO:0071039 nuclear polyadenylation-dependent CUT catabolic process
Cellular Component
GO:0000176 nuclear exosome (RNase complex)
GO:0000177 cytoplasmic exosome (RNase complex)
GO:0000178 exosome (RNase complex)
GO:0005634 nucleus
GO:0005730 nucleolus
GO:0005737 cytoplasm
GO:0005739 mitochondrion

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5vzj, PDBe:5vzj, PDBj:5vzj
PDBsum5vzj
PubMed28742025
UniProtQ08162|RRP44_YEAST Exosome complex exonuclease DIS3 (Gene Name=DIS3)

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