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8B3N

Human Aldose Reductase Mutant A299G/L300G in Complex with a Ligand with an IDD Structure (3-({[2-(carboxymethoxy)-4-fluorobenzoyl]amino}methyl)benzoic acid)

Functional Information from GO Data
ChainGOidnamespacecontents
A0001523biological_processretinoid metabolic process
A0001758molecular_functionretinal dehydrogenase (NAD+) activity
A0002070biological_processepithelial cell maturation
A0003091biological_processrenal water homeostasis
A0004032molecular_functionaldose reductase (NADPH) activity
A0005515molecular_functionprotein binding
A0005615cellular_componentextracellular space
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006629biological_processlipid metabolic process
A0006693biological_processprostaglandin metabolic process
A0006700biological_processC21-steroid hormone biosynthetic process
A0009055molecular_functionelectron transfer activity
A0016491molecular_functionoxidoreductase activity
A0035809biological_processregulation of urine volume
A0036130molecular_functionprostaglandin H2 endoperoxidase reductase activity
A0042572biological_processretinol metabolic process
A0043066biological_processnegative regulation of apoptotic process
A0043795molecular_functionglyceraldehyde oxidoreductase activity
A0044597biological_processdaunorubicin metabolic process
A0044598biological_processdoxorubicin metabolic process
A0046370biological_processfructose biosynthetic process
A0047655molecular_functionallyl-alcohol dehydrogenase activity
A0047939molecular_functionL-glucuronate reductase activity
A0047956molecular_functionglycerol dehydrogenase (NADP+) activity
A0052650molecular_functionall-trans-retinol dehydrogenase (NADP+) activity
A0070062cellular_componentextracellular exosome
A0071475biological_processcellular hyperosmotic salinity response
A0072205biological_processmetanephric collecting duct development
Functional Information from PROSITE/UniProt
site_idPS00062
Number of Residues18
DetailsALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. MeelvdeglVKAIGISNF
ChainResidueDetails
AMET144-PHE161

site_idPS00063
Number of Residues16
DetailsALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. IPKSVTpeRIaENfKV
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":"PubMed","id":"15272156","evidenceCode":"ECO:0000269"}]}
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":"PubMed","id":"15146478","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15272156","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16337231","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17368668","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17418233","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17505104","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Lowers pKa of active site Tyr"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"8281941","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P07943","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 725
ChainResidueDetails
AASP43electrostatic stabiliser
ATYR48proton acceptor, proton donor
ALYS77electrostatic stabiliser, modifies pKa
AHIS110electrostatic stabiliser

238582

PDB entries from 2025-07-09

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