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5N2V

Changes in conformational equilibria regulate the activity of the Dcp2 decapping enzyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0000184biological_processnuclear-transcribed mRNA catabolic process, nonsense-mediated decay
A0000290biological_processdeadenylation-dependent decapping of nuclear-transcribed mRNA
A0000932cellular_componentP-body
A0000956biological_processnuclear-transcribed mRNA catabolic process
A0003723molecular_functionRNA binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006397biological_processmRNA processing
A0008047molecular_functionenzyme activator activity
A0010494cellular_componentcytoplasmic stress granule
A0043085biological_processpositive regulation of catalytic activity
A0043229cellular_componentintracellular organelle
A0098745cellular_componentRNA decapping complex
A0110156biological_processmRNA methylguanosine-cap decapping
A0170008molecular_functionmRNA phosphatase activator activity
B0000184biological_processnuclear-transcribed mRNA catabolic process, nonsense-mediated decay
B0000290biological_processdeadenylation-dependent decapping of nuclear-transcribed mRNA
B0003723molecular_functionRNA binding
B0016787molecular_functionhydrolase activity
B0030145molecular_functionmanganese ion binding
B0140933molecular_function5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity
D0000184biological_processnuclear-transcribed mRNA catabolic process, nonsense-mediated decay
D0000290biological_processdeadenylation-dependent decapping of nuclear-transcribed mRNA
D0000932cellular_componentP-body
D0000956biological_processnuclear-transcribed mRNA catabolic process
D0003723molecular_functionRNA binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006397biological_processmRNA processing
D0008047molecular_functionenzyme activator activity
D0010494cellular_componentcytoplasmic stress granule
D0043085biological_processpositive regulation of catalytic activity
D0043229cellular_componentintracellular organelle
D0098745cellular_componentRNA decapping complex
D0110156biological_processmRNA methylguanosine-cap decapping
D0170008molecular_functionmRNA phosphatase activator activity
E0000184biological_processnuclear-transcribed mRNA catabolic process, nonsense-mediated decay
E0000290biological_processdeadenylation-dependent decapping of nuclear-transcribed mRNA
E0003723molecular_functionRNA binding
E0016787molecular_functionhydrolase activity
E0030145molecular_functionmanganese ion binding
E0140933molecular_function5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue MG B 301
ChainResidue
BGLU143
BGLU146
BMG302
BM7G304

site_idAC2
Number of Residues6
Detailsbinding site for residue MG B 302
ChainResidue
BM7G304
BGLU143
BGLU146
BGLU147
BGLU192
BMG301

site_idAC3
Number of Residues4
Detailsbinding site for residue MG B 303
ChainResidue
BLYS127
BGLU147
BGLU192
BM7G304

site_idAC4
Number of Residues13
Detailsbinding site for residue M7G B 304
ChainResidue
BTRP43
BASP47
BLYS127
BGLY128
BLYS129
BGLU143
BGLU147
BARG190
BLYS191
BGLU192
BMG301
BMG302
BMG303

site_idAC5
Number of Residues4
Detailsbinding site for residue MG E 301
ChainResidue
ELYS127
EGLU147
EGLU192
EM7G304

site_idAC6
Number of Residues6
Detailsbinding site for residue MG E 302
ChainResidue
EGLU143
EGLU146
EGLU147
EGLU192
EMG303
EM7G304

site_idAC7
Number of Residues4
Detailsbinding site for residue MG E 303
ChainResidue
EGLU143
EGLU146
EMG302
EM7G304

site_idAC8
Number of Residues13
Detailsbinding site for residue M7G E 304
ChainResidue
ETRP43
EASP47
ELYS127
EGLY128
ELYS129
EGLU143
EGLU147
EARG190
ELYS191
EGLU192
EMG301
EMG302
EMG303

Functional Information from PROSITE/UniProt
site_idPS00893
Number of Residues22
DetailsNUDIX_BOX Nudix box signature. GkidkdEsdvdCAiREVyEEtG
ChainResidueDetails
BGLY128-GLY149

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING:
ChainResidueDetails
BARG167
BTYR220
EARG167
ETYR220

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PDB entries from 2024-07-10

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