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

4GSF

The structure analysis of cysteine free insulin degrading enzyme (ide) with (s)-2-{2-[carboxymethyl-(3-phenyl-propionyl)-amino]-acetylamino}-3-(3h-imidazol-4-yl)-propionic acid methyl ester

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001540molecular_functionamyloid-beta binding
A0001618molecular_functionvirus receptor activity
A0003824molecular_functioncatalytic activity
A0004175molecular_functionendopeptidase activity
A0004222molecular_functionmetalloendopeptidase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005777cellular_componentperoxisome
A0005782cellular_componentperoxisomal matrix
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0008286biological_processinsulin receptor signaling pathway
A0009897cellular_componentexternal side of plasma membrane
A0009986cellular_componentcell surface
A0010815biological_processbradykinin catabolic process
A0010992biological_processubiquitin recycling
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
A0017046molecular_functionpeptide hormone binding
A0019885biological_processantigen processing and presentation of endogenous peptide antigen via MHC class I
A0030163biological_processprotein catabolic process
A0031597cellular_componentcytosolic proteasome complex
A0031626molecular_functionbeta-endorphin binding
A0032092biological_processpositive regulation of protein binding
A0042277molecular_functionpeptide binding
A0042447biological_processhormone catabolic process
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0043171biological_processpeptide catabolic process
A0043559molecular_functioninsulin binding
A0044877molecular_functionprotein-containing complex binding
A0045732biological_processpositive regulation of protein catabolic process
A0045861biological_processnegative regulation of proteolysis
A0046718biological_processsymbiont entry into host cell
A0046872molecular_functionmetal ion binding
A0050435biological_processamyloid-beta metabolic process
A0051603biological_processproteolysis involved in protein catabolic process
A0070062cellular_componentextracellular exosome
A0097242biological_processamyloid-beta clearance
A0150094biological_processamyloid-beta clearance by cellular catabolic process
A1901142biological_processinsulin metabolic process
A1901143biological_processinsulin catabolic process
A1903715biological_processregulation of aerobic respiration
B0000166molecular_functionnucleotide binding
B0001540molecular_functionamyloid-beta binding
B0001618molecular_functionvirus receptor activity
B0003824molecular_functioncatalytic activity
B0004175molecular_functionendopeptidase activity
B0004222molecular_functionmetalloendopeptidase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005777cellular_componentperoxisome
B0005782cellular_componentperoxisomal matrix
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0008286biological_processinsulin receptor signaling pathway
B0009897cellular_componentexternal side of plasma membrane
B0009986cellular_componentcell surface
B0010815biological_processbradykinin catabolic process
B0010992biological_processubiquitin recycling
B0016020cellular_componentmembrane
B0016323cellular_componentbasolateral plasma membrane
B0016787molecular_functionhydrolase activity
B0016887molecular_functionATP hydrolysis activity
B0017046molecular_functionpeptide hormone binding
B0019885biological_processantigen processing and presentation of endogenous peptide antigen via MHC class I
B0030163biological_processprotein catabolic process
B0031597cellular_componentcytosolic proteasome complex
B0031626molecular_functionbeta-endorphin binding
B0032092biological_processpositive regulation of protein binding
B0042277molecular_functionpeptide binding
B0042447biological_processhormone catabolic process
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0043171biological_processpeptide catabolic process
B0043559molecular_functioninsulin binding
B0044877molecular_functionprotein-containing complex binding
B0045732biological_processpositive regulation of protein catabolic process
B0045861biological_processnegative regulation of proteolysis
B0046718biological_processsymbiont entry into host cell
B0046872molecular_functionmetal ion binding
B0050435biological_processamyloid-beta metabolic process
B0051603biological_processproteolysis involved in protein catabolic process
B0070062cellular_componentextracellular exosome
B0097242biological_processamyloid-beta clearance
B0150094biological_processamyloid-beta clearance by cellular catabolic process
B1901142biological_processinsulin metabolic process
B1901143biological_processinsulin catabolic process
B1903715biological_processregulation of aerobic respiration
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MGH A 1101
ChainResidue
AHIS332
AHIS336
AGLY339
AGLU341
ALEU359
AVAL360
AGLY361
ATYR609
AHOH1267

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 1102
ChainResidue
AHIS108
AHIS112
AGLU189

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MGH B 1101
ChainResidue
BHIS332
BGLY339
BGLU341
BLEU359
BVAL360
BGLY361
BGLN363
BHOH1216

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN B 1102
ChainResidue
BHIS108
BHIS112
BGLU189

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsMotif: {"description":"SlyX motif","evidences":[{"source":"UniProtKB","id":"Q9JHR7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10096","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10684867","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17051221","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19321446","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"23922390","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10096","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17051221","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17613531","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18986166","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19321446","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2G54","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JG4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CWW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3N56","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3N57","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsBinding site: {"description":"in the exosite"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18986166","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P35559","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9JHR7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

PDB statisticsPDBj update infoContact PDBjnumon