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5UXF

Crystal Structure of mouse RECON (AKR1C13) in complex with Cyclic di-AMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0001758molecular_functionretinal dehydrogenase (NAD+) activity
A0004032molecular_functionaldose reductase (NADPH) activity
A0004745molecular_functionall-trans-retinol dehydrogenase (NAD+) activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005829cellular_componentcytosol
A0006693biological_processprostaglandin metabolic process
A0006805biological_processxenobiotic metabolic process
A0008106molecular_functionalcohol dehydrogenase (NADP+) activity
A0016491molecular_functionoxidoreductase activity
A0016655molecular_functionoxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor
A0031406molecular_functioncarboxylic acid binding
A0032052molecular_functionbile acid binding
A0036130molecular_functionprostaglandin H2 endoperoxidase reductase activity
A0036131molecular_functionprostaglandin D2 11-ketoreductase activity
A0042448biological_processprogesterone metabolic process
A0044597biological_processdaunorubicin metabolic process
A0044598biological_processdoxorubicin metabolic process
A0045550molecular_functiongeranylgeranyl reductase activity
A0045703molecular_functionketoreductase activity
A0047020molecular_function15-hydroxyprostaglandin-D dehydrogenase (NADP+) activity
A0047023molecular_functionandrosterone dehydrogenase [NAD(P)+] activity
A0047045molecular_functiontestosterone dehydrogenase (NADP+) activity
A0047086molecular_functionketosteroid monooxygenase activity
A0047115molecular_functiontrans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity
A0047743molecular_functionchlordecone reductase activity
A0047787molecular_functionDelta4-3-oxosteroid 5beta-reductase activity
A0140169molecular_function3-alpha-hydroxysteroid 3-dehydrogenase [NAD(P)+] activity
Functional Information from PDB Data
site_idAC1
Number of Residues25
Detailsbinding site for residue 2BA A 401
ChainResidue
ATYR24
AGLN270
ASER271
AGLU276
AGLU279
AASN280
AHOH506
AHOH536
AHOH538
AHOH539
AHOH547
ATYR55
AHOH552
AHOH554
AHOH608
AHOH643
AHOH660
AHOH771
ATYR216
AGLY217
AALA218
ALEU219
AGLY220
ATHR221
AALA253

Functional Information from PROSITE/UniProt
site_idPS00062
Number of Residues18
DetailsALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. LeeckdaglVKSIGVSNF
ChainResidueDetails
ALEU151-PHE168

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

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

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsSite: {"description":"Lowers pKa of active site Tyr","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of putative reductase (NP_038806.2) from Mus musculus at 1.18 A resolution.","authoringGroup":["Joint center for structural genomics (JCSG)"]}}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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