Structure of PDB 5n2v Chain E Binding Site BS02
Receptor Information
>5n2v Chain E (length=223) Species:
4896
(Schizosaccharomyces pombe) [
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SFTNATFSQVLDDLSARFILNLPAEEQSSVERLCFQIEQAHWFYEDFIRA
QNDQLPSLGLRVFSAKLFAHCPLLWKWSKVHEEAFDDFLRYKTRIPVRGA
IMLDMSMQQCVLVKGWKASSGWGFPKGKIDKDESDVDCAIREVYEETGFD
CSSRINPNEFIDMTIRGQNVRLYIIPGISLDTRFESRTRKEISKIEWHNL
MDLPTFYMVIPFLAPLKKWIKKR
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
5n2v Chain E Residue 301 [
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Receptor-Ligand Complex Structure
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PDB
5n2v
Changes in conformational equilibria regulate the activity of the Dcp2 decapping enzyme.
Resolution
3.1 Å
Binding residue
(original residue number in PDB)
K127 E147
Binding residue
(residue number reindexed from 1)
K126 E146
Annotation score
1
Enzymatic activity
Enzyme Commision number
3.-.-.-
Gene Ontology
Molecular Function
GO:0003723
RNA binding
GO:0016787
hydrolase activity
GO:0030145
manganese ion binding
GO:0140933
5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity
Biological Process
GO:0000184
nuclear-transcribed mRNA catabolic process, nonsense-mediated decay
GO:0000290
deadenylation-dependent decapping of nuclear-transcribed mRNA
View graph for
Molecular Function
View graph for
Biological Process
External links
PDB
RCSB:5n2v
,
PDBe:5n2v
,
PDBj:5n2v
PDBsum
5n2v
PubMed
28533364
UniProt
O13828
|DCP2_SCHPO mRNA decapping complex subunit 2 (Gene Name=dcp2)
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