Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5EBB

Structure of human sphingomyelinase phosphodiesterase like 3A (SMPDL3A) with Zn2+

Functional Information from GO Data
ChainGOidnamespacecontents
A0004767molecular_functionsphingomyelin phosphodiesterase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006685biological_processsphingomyelin catabolic process
A0008081molecular_functionphosphoric diester hydrolase activity
A0008270molecular_functionzinc ion binding
A0009143biological_processnucleoside triphosphate catabolic process
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
A0017111molecular_functionribonucleoside triphosphate phosphatase activity
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
A0160049biological_processnegative regulation of cGAS/STING signaling pathway
B0004767molecular_functionsphingomyelin phosphodiesterase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0006685biological_processsphingomyelin catabolic process
B0008081molecular_functionphosphoric diester hydrolase activity
B0008270molecular_functionzinc ion binding
B0009143biological_processnucleoside triphosphate catabolic process
B0016787molecular_functionhydrolase activity
B0016887molecular_functionATP hydrolysis activity
B0017111molecular_functionribonucleoside triphosphate phosphatase activity
B0046872molecular_functionmetal ion binding
B0070062cellular_componentextracellular exosome
B0160049biological_processnegative regulation of cGAS/STING signaling pathway
C0004767molecular_functionsphingomyelin phosphodiesterase activity
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0006685biological_processsphingomyelin catabolic process
C0008081molecular_functionphosphoric diester hydrolase activity
C0008270molecular_functionzinc ion binding
C0009143biological_processnucleoside triphosphate catabolic process
C0016787molecular_functionhydrolase activity
C0016887molecular_functionATP hydrolysis activity
C0017111molecular_functionribonucleoside triphosphate phosphatase activity
C0046872molecular_functionmetal ion binding
C0070062cellular_componentextracellular exosome
C0160049biological_processnegative regulation of cGAS/STING signaling pathway
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues21
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26783088","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26783088","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26783088","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28104755","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26783088","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28104755","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26783088","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28104755","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

245011

PDB entries from 2025-11-19

PDB statisticsPDBj update infoContact PDBjnumon