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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6SH2

Crystal structure of human neprilysin E584D in complex with C-type natriuretic peptide.

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AAA0001786molecular_functionphosphatidylserine binding
AAA0001822biological_processkidney development
AAA0001890biological_processplacenta development
AAA0002003biological_processangiotensin maturation
AAA0004175molecular_functionendopeptidase activity
AAA0004181molecular_functionmetallocarboxypeptidase activity
AAA0004222molecular_functionmetalloendopeptidase activity
AAA0005515molecular_functionprotein binding
AAA0005576cellular_componentextracellular region
AAA0005654cellular_componentnucleoplasm
AAA0005737cellular_componentcytoplasm
AAA0005769cellular_componentearly endosome
AAA0005802cellular_componenttrans-Golgi network
AAA0005813cellular_componentcentrosome
AAA0005829cellular_componentcytosol
AAA0005886cellular_componentplasma membrane
AAA0005903cellular_componentbrush border
AAA0005925cellular_componentfocal adhesion
AAA0006508biological_processproteolysis
AAA0006518biological_processpeptide metabolic process
AAA0007611biological_processlearning or memory
AAA0008021cellular_componentsynaptic vesicle
AAA0008233molecular_functionpeptidase activity
AAA0008237molecular_functionmetallopeptidase activity
AAA0008238molecular_functionexopeptidase activity
AAA0008270molecular_functionzinc ion binding
AAA0009986cellular_componentcell surface
AAA0010814biological_processsubstance P catabolic process
AAA0010815biological_processbradykinin catabolic process
AAA0016020cellular_componentmembrane
AAA0016485biological_processprotein processing
AAA0016787molecular_functionhydrolase activity
AAA0019233biological_processsensory perception of pain
AAA0030163biological_processprotein catabolic process
AAA0030324biological_processlung development
AAA0030424cellular_componentaxon
AAA0030425cellular_componentdendrite
AAA0030667cellular_componentsecretory granule membrane
AAA0031410cellular_componentcytoplasmic vesicle
AAA0036064cellular_componentciliary basal body
AAA0042277molecular_functionpeptide binding
AAA0042447biological_processhormone catabolic process
AAA0042803molecular_functionprotein homodimerization activity
AAA0043025cellular_componentneuronal cell body
AAA0043627biological_processresponse to estrogen
AAA0044306cellular_componentneuron projection terminus
AAA0045121cellular_componentmembrane raft
AAA0045202cellular_componentsynapse
AAA0046449biological_processcreatinine metabolic process
AAA0046872molecular_functionmetal ion binding
AAA0050435biological_processamyloid-beta metabolic process
AAA0050769biological_processpositive regulation of neurogenesis
AAA0061837biological_processneuropeptide processing
AAA0070012molecular_functionoligopeptidase activity
AAA0070062cellular_componentextracellular exosome
AAA0071345biological_processcellular response to cytokine stimulus
AAA0071492biological_processcellular response to UV-A
AAA0071493biological_processcellular response to UV-B
AAA0090399biological_processreplicative senescence
AAA0097242biological_processamyloid-beta clearance
AAA0098793cellular_componentpresynapse
AAA0150094biological_processamyloid-beta clearance by cellular catabolic process
AAA1900273biological_processpositive regulation of long-term synaptic potentiation
AAA1901612molecular_functioncardiolipin binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues694
DetailsDomain: {"description":"Peptidase M13","evidences":[{"source":"PROSITE-ProRule","id":"PRU01233","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01233","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01233","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8168535","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P07861","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01233","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10669592","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14747736","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17704566","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10669592","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14747736","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17704566","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10669592","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14747736","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17704566","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22766194","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 623
ChainResidueDetails

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PDB entries from 2025-07-09

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