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4WGK

Crystal structure of human neutral ceramidase with Zn-bound phosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0017040molecular_functionN-acylsphingosine amidohydrolase activity
A0046514biological_processceramide catabolic process
B0017040molecular_functionN-acylsphingosine amidohydrolase activity
B0046514biological_processceramide catabolic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsRegion: {"description":"Required for correct folding and localization","evidences":[{"source":"UniProtKB","id":"Q91XT9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"16229686","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26190575","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4WGK","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues10
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"26190575","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4WGK","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (GalNAc...) threonine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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PDB entries from 2026-01-21

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