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1EKO

PIG ALDOSE REDUCTASE COMPLEXED WITH IDD384 INHIBITOR

Functional Information from GO Data
ChainGOidnamespacecontents
A0001523biological_processretinoid metabolic process
A0001758molecular_functionretinal dehydrogenase (NAD+) activity
A0004032molecular_functionaldose reductase (NADPH) activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006693biological_processprostaglandin metabolic process
A0016491molecular_functionoxidoreductase activity
A0036130molecular_functionprostaglandin H2 endoperoxidase reductase activity
A0042572biological_processretinol metabolic process
A0047655molecular_functionallyl-alcohol dehydrogenase activity
A0047956molecular_functionglycerol dehydrogenase (NADP+) activity
A0052650molecular_functionall-trans-retinol dehydrogenase (NADP+) activity
Functional Information from PDB Data
site_idAC1
Number of Residues29
DetailsBINDING SITE FOR RESIDUE NAP A 318
ChainResidue
AGLY18
AGLN183
ATYR209
ASER210
APRO211
ALEU212
AGLY213
ASER214
AASP216
AALA245
AILE260
ATHR19
APRO261
ALYS262
ASER263
AVAL264
ATHR265
AARG268
AGLU271
AASN272
AI84320
AHOH555
ATRP20
ALYS21
AASP43
ATYR48
AHIS110
ASER159
AASN160

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE I84 A 320
ChainResidue
ATRP20
AVAL47
ATYR48
ATRP79
AHIS110
ATRP111
APHE122
APRO218
ATRP219
ANAP318

Functional Information from PROSITE/UniProt
site_idPS00062
Number of Residues18
DetailsALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. MeelvdeglVKAIGVSNF
ChainResidueDetails
AMET144-PHE161

site_idPS00063
Number of Residues16
DetailsALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. IPKSVTpeRIaENfQV
ChainResidueDetails
AILE260-VAL275

site_idPS00798
Number of Residues18
DetailsALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRHIDCAhvyqnEneVG
ChainResidueDetails
AGLY38-GLY55

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P15121","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues62
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P15121","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Lowers pKa of active site Tyr","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P07943","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P15121","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mrq
ChainResidueDetails
ATYR48
AASP43
AHIS110
ALYS77

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mrq
ChainResidueDetails
ATYR48
ALYS77

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PDB entries from 2025-07-16

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