Structure of PDB 5n2v Chain E Binding Site BS01

Receptor Information
>5n2v Chain E (length=223) Species: 4896 (Schizosaccharomyces pombe) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SFTNATFSQVLDDLSARFILNLPAEEQSSVERLCFQIEQAHWFYEDFIRA
QNDQLPSLGLRVFSAKLFAHCPLLWKWSKVHEEAFDDFLRYKTRIPVRGA
IMLDMSMQQCVLVKGWKASSGWGFPKGKIDKDESDVDCAIREVYEETGFD
CSSRINPNEFIDMTIRGQNVRLYIIPGISLDTRFESRTRKEISKIEWHNL
MDLPTFYMVIPFLAPLKKWIKKR
Ligand information
>5n2v Chain F (length=23) Species: 4896 (Schizosaccharomyces pombe) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
ILYAGPTFTHSPAASNLPIPTFL
Receptor-Ligand Complex Structure
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PDB5n2v Changes in conformational equilibria regulate the activity of the Dcp2 decapping enzyme.
Resolution3.1 Å
Binding residue
(original residue number in PDB)		P24 E27 R33 F36 Y92 I96 K129 I130 D131 K132 R142
Binding residue
(residue number reindexed from 1)		P23 E26 R32 F35 Y91 I95 K128 I129 D130 K131 R141
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

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Molecular Function
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Biological Process
External links
PDB RCSB:5n2v, PDBe:5n2v, PDBj:5n2v
PDBsum5n2v
PubMed28533364
UniProtO13828|DCP2_SCHPO mRNA decapping complex subunit 2 (Gene Name=dcp2)

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