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1DMT

STRUCTURE OF HUMAN NEUTRAL ENDOPEPTIDASE COMPLEXED WITH PHOSPHORAMIDON

Functional Information from GO Data
ChainGOidnamespacecontents
A0001786molecular_functionphosphatidylserine binding
A0001822biological_processkidney development
A0001890biological_processplacenta development
A0004175molecular_functionendopeptidase activity
A0004222molecular_functionmetalloendopeptidase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005769cellular_componentearly endosome
A0005802cellular_componenttrans-Golgi network
A0005886cellular_componentplasma membrane
A0005903cellular_componentbrush border
A0005925cellular_componentfocal adhesion
A0006508biological_processproteolysis
A0006518biological_processpeptide metabolic process
A0007611biological_processlearning or memory
A0008021cellular_componentsynaptic vesicle
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008238molecular_functionexopeptidase activity
A0008270molecular_functionzinc ion binding
A0009986cellular_componentcell surface
A0010814biological_processsubstance P catabolic process
A0010815biological_processbradykinin catabolic process
A0016020cellular_componentmembrane
A0016485biological_processprotein processing
A0019233biological_processsensory perception of pain
A0030163biological_processprotein catabolic process
A0030324biological_processlung development
A0030424cellular_componentaxon
A0030425cellular_componentdendrite
A0030667cellular_componentsecretory granule membrane
A0031410cellular_componentcytoplasmic vesicle
A0042277molecular_functionpeptide binding
A0042447biological_processhormone catabolic process
A0042803molecular_functionprotein homodimerization activity
A0043025cellular_componentneuronal cell body
A0043627biological_processresponse to estrogen
A0044306cellular_componentneuron projection terminus
A0045121cellular_componentmembrane raft
A0045202cellular_componentsynapse
A0046449biological_processcreatinine metabolic process
A0046872molecular_functionmetal ion binding
A0050435biological_processamyloid-beta metabolic process
A0050769biological_processpositive regulation of neurogenesis
A0061837biological_processneuropeptide processing
A0070012molecular_functionoligopeptidase activity
A0070062cellular_componentextracellular exosome
A0071345biological_processcellular response to cytokine stimulus
A0071492biological_processcellular response to UV-A
A0071493biological_processcellular response to UV-B
A0090399biological_processreplicative senescence
A0097242biological_processamyloid-beta clearance
A0098793cellular_componentpresynapse
A0150094biological_processamyloid-beta clearance by cellular catabolic process
A1900273biological_processpositive regulation of long-term synaptic potentiation
A1901612molecular_functioncardiolipin binding
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VIGHEITHGF
ChainResidueDetails
AVAL580-PHE589

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000255|PROSITE-ProRule:PRU10095
ChainResidueDetails
AGLU584

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000269|PubMed:8168535
ChainResidueDetails
AASP650

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P07861
ChainResidueDetails
AARG102

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01233
ChainResidueDetails
AHIS583
AHIS587
AGLU646

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10669592, ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14747736, ECO:0000269|PubMed:17704566
ChainResidueDetails
AASN144

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519
ChainResidueDetails
AASN284

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10669592, ECO:0000269|PubMed:14747736, ECO:0000269|PubMed:17704566
ChainResidueDetails
AASN324

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10669592, ECO:0000269|PubMed:14747736, ECO:0000269|PubMed:17704566, ECO:0000269|PubMed:22766194
ChainResidueDetails
AASN627

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1r1j
ChainResidueDetails
AGLU584
AARG717
AHIS711
AASP650

site_idMCSA1
Number of Residues7
DetailsM-CSA 623
ChainResidueDetails
AHIS583metal ligand
AGLU584proton shuttle (general acid/base)
AHIS587metal ligand
AGLU646metal ligand
AASP650electrostatic stabiliser
AHIS711electrostatic stabiliser
AARG717electrostatic stabiliser

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PDB entries from 2024-10-30

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