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5UXF

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0004033molecular_functionaldo-keto reductase (NADPH) activity
A0006805biological_processxenobiotic metabolic process
A0016491molecular_functionoxidoreductase 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
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
ATYR55

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|Ref.6
ChainResidueDetails
AGLY20
AASP50
ATYR55
ASER166
AGLN190
ATYR216
AGLN270

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

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Lowers pKa of active site Tyr => ECO:0000250
ChainResidueDetails
ALYS84

226707

PDB entries from 2024-10-30

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