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1AE4

ALDEHYDE REDUCTASE COMPLEXED WITH COFACTOR AND INHIBITOR, ALPHA CARBON ATOMS ONLY

Functional Information from GO Data
ChainGOidnamespacecontents
A0004032molecular_functionaldose reductase (NADPH) activity
A0004745molecular_functionall-trans-retinol dehydrogenase (NAD+) activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006629biological_processlipid metabolic process
A0008106molecular_functionalcohol dehydrogenase (NADP+) activity
A0016020cellular_componentmembrane
A0016324cellular_componentapical plasma membrane
A0016491molecular_functionoxidoreductase activity
A0019853biological_processL-ascorbic acid biosynthetic process
A0042840biological_processD-glucuronate catabolic process
A0046185biological_processaldehyde catabolic process
A0047655molecular_functionallyl-alcohol dehydrogenase activity
A0047939molecular_functionL-glucuronate reductase activity
A0047941molecular_functionglucuronolactone reductase activity
A0047956molecular_functionglycerol dehydrogenase [NADP+] activity
A0110095biological_processcellular detoxification of aldehyde
A1990002molecular_functionmethylglyoxal reductase (NADPH) (acetol producing) activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NAP A 350
ChainResidue
AGLY20
ATRP22
ASER211
ALEU213
ASER215
APRO262
ASER264
ATOL600

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE TOL A 600
ChainResidue
ANAP350

Functional Information from PROSITE/UniProt
site_idPS00062
Number of Residues18
DetailsALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. LealvakglVRALGLSNF
ChainResidueDetails
ALEU147-PHE164

site_idPS00063
Number of Residues16
DetailsALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. IPKSVTpsRIpQNiQV
ChainResidueDetails
AILE261-VAL276

site_idPS00798
Number of Residues18
DetailsALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRHIDCAaiygnEleIG
ChainResidueDetails
AGLY40-GLY57

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:7552731
ChainResidueDetails
AGLY51

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AGLN12

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:O60218
ChainResidueDetails
ATRP22
ACYS46
AASN163
AVAL185

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:7552731
ChainResidueDetails
ATRP114
APRO212

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Lowers pKa of active site Tyr => ECO:0000250|UniProtKB:P14550
ChainResidueDetails
ALEU81

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P14550
ChainResidueDetails
AALA3

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P51635
ChainResidueDetails
ACYS5

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9JII6
ChainResidueDetails
AASN128

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9JII6
ChainResidueDetails
AALA146

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P14550
ChainResidueDetails
APRO212

218196

PDB entries from 2024-04-10

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