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4RE9

Crystal structure of human insulin degrading enzyme (IDE) in complex with compound 71290

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide 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
A0008152biological_processmetabolic process
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
A0019885biological_processantigen processing and presentation of endogenous peptide antigen via MHC class I
A0030163biological_processprotein catabolic process
A0032092biological_processpositive regulation of protein binding
A0042277molecular_functionpeptide binding
A0042447biological_processhormone catabolic process
A0042803molecular_functionprotein homodimerization activity
A0043171biological_processpeptide catabolic process
A0043559molecular_functioninsulin binding
A0045732biological_processpositive regulation of protein catabolic process
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
A0140036molecular_functionubiquitin-modified protein reader activity
A0150094biological_processamyloid-beta clearance by cellular catabolic process
A1901142biological_processinsulin metabolic process
A1901143biological_processinsulin catabolic process
A1903715biological_processregulation of aerobic respiration
B0000166molecular_functionnucleotide 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
B0008152biological_processmetabolic process
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
B0019885biological_processantigen processing and presentation of endogenous peptide antigen via MHC class I
B0030163biological_processprotein catabolic process
B0032092biological_processpositive regulation of protein binding
B0042277molecular_functionpeptide binding
B0042447biological_processhormone catabolic process
B0042803molecular_functionprotein homodimerization activity
B0043171biological_processpeptide catabolic process
B0043559molecular_functioninsulin binding
B0045732biological_processpositive regulation of protein catabolic process
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
B0140036molecular_functionubiquitin-modified protein reader activity
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 Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1101
ChainResidue
AHIS108
AHIS112
AGLU189
A3M91102

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 3M9 A 1102
ChainResidue
AASN139
AALA140
AGLU189
AARG824
ATYR831
AZN1101
APEG1104
AHIS108
AGLU111
AHIS112
APHE115
ASER128

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EPE A 1103
ChainResidue
AGLN800
AARG839
AALA840
AASN841
AGLY842

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PEG A 1104
ChainResidue
AHIS679
A3M91102

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG A 1105
ChainResidue
ASER590
AASN622
ATYR666

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PEG A 1106
ChainResidue
AARG477

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG A 1107
ChainResidue
AALA198
ATRP199
APHE202

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG A 1108
ChainResidue
AVAL360
AGLY361
AGLN363

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG A 1109
ChainResidue
ATHR358
AVAL360
AASN376

site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 1PE A 1110
ChainResidue
AGLN323
ATYR326
AASN329
AHIS332
AASN418
ATYR444
AALA452
AGLU453
ATYR454

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1101
ChainResidue
BHIS108
BHIS112
BGLU189
B3M91102

site_idBC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 3M9 B 1102
ChainResidue
BHIS108
BGLU111
BHIS112
BSER128
BASN139
BALA140
BGLU189
BARG824
BTYR831
BZN1101

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EPE B 1103
ChainResidue
BGLN800
BARG839
BALA840
BASN841
BGLY842
BSER913
BARG920
BHOH1207

site_idBC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PEG B 1104
ChainResidue
BPEG1105

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PEG B 1105
ChainResidue
BGLY339
BGLU341
BLEU359
BVAL360
BGLY361
BPEG1104

site_idBC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PEG B 1106
ChainResidue
BMET683
BARG847

site_idBC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PEG B 1107
ChainResidue
BALA198
BTRP199

site_idBC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE 1PE B 1108
ChainResidue
BSER590
BASN622
BSER669
BLYS697

site_idCC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO B 1109
ChainResidue
BGLN621

Functional Information from PROSITE/UniProt
site_idPS00143
Number of Residues24
DetailsINSULINASE Insulinase family, zinc-binding region signature. GslsdppniaGlSHFLEHMlFlGT
ChainResidueDetails
AGLY95-THR118

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000305|PubMed:10684867, ECO:0000305|PubMed:17051221, ECO:0000305|PubMed:19321446, ECO:0000305|PubMed:23922390
ChainResidueDetails
AGLU111
BGLU111

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57
ChainResidueDetails
AHIS108
AHIS112
AGLU189
BHIS108
BHIS112
BGLU189

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: in the exosite
ChainResidueDetails
AHIS336
BHIS336

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:18986166
ChainResidueDetails
ALEU359
BLEU359

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P35559
ChainResidueDetails
AARG429
AASP895
BARG429
BASP895

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7
ChainResidueDetails
ALYS192
ALYS697
BLYS192
BLYS697

218853

PDB entries from 2024-04-24

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