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7EG4

Cryo-EM structure of nauclefine-induced PDE3A-SLFN12 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004114molecular_function3',5'-cyclic-nucleotide phosphodiesterase activity
A0007165biological_processsignal transduction
A0008081molecular_functionphosphoric diester hydrolase activity
B0004540molecular_functionRNA nuclease activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0016075biological_processrRNA catabolic process
B0016787molecular_functionhydrolase activity
B0043022molecular_functionribosome binding
B0097190biological_processapoptotic signaling pathway
C0004114molecular_function3',5'-cyclic-nucleotide phosphodiesterase activity
C0007165biological_processsignal transduction
C0008081molecular_functionphosphoric diester hydrolase activity
D0004540molecular_functionRNA nuclease activity
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0016075biological_processrRNA catabolic process
D0016787molecular_functionhydrolase activity
D0043022molecular_functionribosome binding
D0097190biological_processapoptotic signaling pathway
Functional Information from PROSITE/UniProt
site_idPS00126
Number of Residues12
DetailsPDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDYdHpGrtNaF
ChainResidueDetails
CHIS836-PHE847

site_idPS00216
Number of Residues17
DetailsSUGAR_TRANSPORT_1 Sugar transport proteins signature 1. IFDLVENIGRKcgril.S
ChainResidueDetails
CILE696-SER712

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:35104454
ChainResidueDetails
DSER368
BSER368

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:34272366, ECO:0007744|PDB:7L29
ChainResidueDetails
CHIS752
CGLN1001
AHIS752
AGLN1001

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:34272366, ECO:0007744|PDB:7KWE, ECO:0007744|PDB:7L27, ECO:0007744|PDB:7L28, ECO:0007744|PDB:7L29
ChainResidueDetails
CHIS756
CHIS836
CASP837
CASP950
AHIS756
AHIS836
AASP837
AASP950

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9Z0X4
ChainResidueDetails
CSER1033
ASER1033

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9Z0X4
ChainResidueDetails
CTHR1036
ATHR1036

222415

PDB entries from 2024-07-10

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