Structure of PDB 5n2v Chain E

Receptor sequence
>5n2vE (length=223) Species: 4896 (Schizosaccharomyces pombe) [Search protein sequence]
SFTNATFSQVLDDLSARFILNLPAEEQSSVERLCFQIEQAHWFYEDFIRA
QNDQLPSLGLRVFSAKLFAHCPLLWKWSKVHEEAFDDFLRYKTRIPVRGA
IMLDMSMQQCVLVKGWKASSGWGFPKGKIDKDESDVDCAIREVYEETGFD
CSSRINPNEFIDMTIRGQNVRLYIIPGISLDTRFESRTRKEISKIEWHNL
MDLPTFYMVIPFLAPLKKWIKKR
3D structure
PDB5n2v Changes in conformational equilibria regulate the activity of the Dcp2 decapping enzyme.
ChainE
Resolution3.1 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.-.-.-
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 peptide E P24 E27 R33 F36 Y92 I96 K129 I130 D131 K132 R142 P23 E26 R32 F35 Y91 I95 K128 I129 D130 K131 R141
BS02 MG E K127 E147 K126 E146
BS03 MG E E143 E147 E192 E142 E146 E191
BS04 8NK E W43 D47 G128 K129 E143 R190 K191 E192 W42 D46 G127 K128 E142 R189 K190 E191
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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