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3UGR

AKR1C3 complex with indomethacin at pH 6.8

Functional Information from GO Data
ChainGOidnamespacecontents
A0001523biological_processretinoid metabolic process
A0001758molecular_functionretinal dehydrogenase activity
A0004032molecular_functionaldose reductase (NADPH) activity
A0004033molecular_functionaldo-keto reductase (NADPH) activity
A0004303molecular_functionestradiol 17-beta-dehydrogenase [NAD(P)+] activity
A0004745molecular_functionall-trans-retinol dehydrogenase (NAD+) activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006693biological_processprostaglandin metabolic process
A0007186biological_processG protein-coupled receptor signaling pathway
A0007584biological_processresponse to nutrient
A0008202biological_processsteroid metabolic process
A0008284biological_processpositive regulation of cell population proliferation
A0008584biological_processmale gonad development
A0009267biological_processcellular response to starvation
A0016488biological_processfarnesol catabolic process
A0016491molecular_functionoxidoreductase activity
A0016655molecular_functionoxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor
A0019371biological_processcyclooxygenase pathway
A0030216biological_processkeratinocyte differentiation
A0032052molecular_functionbile acid binding
A0035410molecular_functionobsolete dihydrotestosterone 17-beta-dehydrogenase activity
A0036130molecular_functionprostaglandin H2 endoperoxidase reductase activity
A0036131molecular_functionprostaglandin D2 11-ketoreductase activity
A0042448biological_processprogesterone metabolic process
A0042572biological_processretinol metabolic process
A0042574biological_processretinal metabolic process
A0043170biological_processmacromolecule metabolic process
A0044597biological_processdaunorubicin metabolic process
A0044598biological_processdoxorubicin metabolic process
A0045550molecular_functiongeranylgeranyl reductase activity
A0045703molecular_functionketoreductase activity
A0047017molecular_functionprostaglandin F synthase activity
A0047020molecular_function15-hydroxyprostaglandin-D dehydrogenase (NADP+) activity
A0047023molecular_functionandrosterone dehydrogenase activity
A0047024molecular_function5alpha-androstane-3beta,17beta-diol dehydrogenase activity
A0047035molecular_functiontestosterone dehydrogenase (NAD+) activity
A0047044molecular_functionandrostan-3-alpha,17-beta-diol dehydrogenase activity
A0047045molecular_functiontestosterone 17-beta-dehydrogenase (NADP+) activity
A0047086molecular_functionketosteroid monooxygenase activity
A0047787molecular_functionDelta4-3-oxosteroid 5beta-reductase activity
A0048385biological_processregulation of retinoic acid receptor signaling pathway
A0051897biological_processpositive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
A0052650molecular_functionall-trans-retinol dehydrogenase (NADP+) activity
A0061370biological_processtestosterone biosynthetic process
A0070062cellular_componentextracellular exosome
A0070293biological_processrenal absorption
A0071277biological_processcellular response to calcium ion
A0071379biological_processcellular response to prostaglandin stimulus
A0071384biological_processcellular response to corticosteroid stimulus
A0071395biological_processcellular response to jasmonic acid stimulus
A0071799biological_processcellular response to prostaglandin D stimulus
A1900053biological_processnegative regulation of retinoic acid biosynthetic process
A2000224biological_processregulation of testosterone biosynthetic process
A2000353biological_processpositive regulation of endothelial cell apoptotic process
A2000379biological_processpositive regulation of reactive oxygen species metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues33
DetailsBINDING SITE FOR RESIDUE NAP A 1001
ChainResidue
AGLY22
ATYR216
ASER217
AALA218
ALEU219
AGLY220
ASER221
AGLN222
ALEU236
AALA253
ALEU268
ATHR23
AALA269
ALYS270
ASER271
ATYR272
AARG276
AGLN279
AASN280
AHOH337
AHOH410
AHOH425
ATYR24
AHOH430
AHOH436
AHOH459
AIMN2001
AASP50
ATYR55
AHIS117
ASER166
AASN167
AGLN190

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE IMN A 2001
ChainResidue
ATYR24
ALEU54
ATYR55
ATRP86
AHIS117
ASER118
AMET120
AASN167
AGLU192
ATYR216
ASER217
ASER221
AGLN222
ATRP227
APHE306
APHE311
ATYR317
ATYR319
AHOH398
AHOH489
ANAP1001
ADMS2002

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DMS A 2002
ChainResidue
ASER118
AMET120
AASN167
APHE306
AIMN2001

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 2004
ChainResidue
APHE15
AGLU77
AASP78
AILE79
APHE80
AASP112
AHOH473

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 2005
ChainResidue
ALEU182
ALYS183
ALYS185
AHOH466
AHOH484
AHOH498

Functional Information from PROSITE/UniProt
site_idPS00062
Number of Residues18
DetailsALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. MekckdaglAKSIGVSNF
ChainResidueDetails
AMET151-PHE168

site_idPS00063
Number of Residues16
DetailsALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. LAKSYNeqRIrQNvQV
ChainResidueDetails
ALEU268-VAL283

site_idPS00798
Number of Residues18
DetailsALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GFRHIDSAhlynnEeqVG
ChainResidueDetails
AGLY45-GLY62

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
ATYR55

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:14979715, ECO:0000269|PubMed:14996743, ECO:0000269|PubMed:15087468
ChainResidueDetails
ATHR23
AASP50
ASER166
AGLN190
ATYR216
ALYS270
AARG276

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AHIS117

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Important for substrate specificity => ECO:0000250
ChainResidueDetails
ALEU54

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Lowers pKa of active site Tyr => ECO:0000250|UniProtKB:P14550
ChainResidueDetails
ALYS84

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Involved in ligand recognition and product release => ECO:0000269|PubMed:15087468
ChainResidueDetails
ATRP227
APHE306

226707

PDB entries from 2024-10-30

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