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5M2F

Crystal structure of human AKR1B10 complexed with NADP+ and the synthetic retinoid UVI2008

Functional Information from GO Data
ChainGOidnamespacecontents
X0001523biological_processretinoid metabolic process
X0001758molecular_functionretinal dehydrogenase activity
X0004032molecular_functionaldose reductase (NADPH) activity
X0004033molecular_functionaldo-keto reductase (NADPH) activity
X0005515molecular_functionprotein binding
X0005576cellular_componentextracellular region
X0005764cellular_componentlysosome
X0005829cellular_componentcytosol
X0006629biological_processlipid metabolic process
X0008106molecular_functionalcohol dehydrogenase (NADP+) activity
X0016488biological_processfarnesol catabolic process
X0016491molecular_functionoxidoreductase activity
X0042572biological_processretinol metabolic process
X0044597biological_processdaunorubicin metabolic process
X0044598biological_processdoxorubicin metabolic process
X0045550molecular_functiongeranylgeranyl reductase activity
X0047655molecular_functionallyl-alcohol dehydrogenase activity
X0047718molecular_functionindanol dehydrogenase activity
X0052650molecular_functionall-trans-retinol dehydrogenase (NADP+) activity
X0110095biological_processcellular detoxification of aldehyde
Functional Information from PDB Data
site_idAC1
Number of Residues35
Detailsbinding site for residue NAP X 401
ChainResidue
XGLY19
XGLN184
XTYR210
XSER211
XPRO212
XLEU213
XGLY214
XSER215
XPRO216
XASP217
XALA246
XTHR20
XILE261
XPRO262
XMLY263
XSER264
XVAL265
XTHR266
XARG269
XGLU272
XASN273
XUV8402
XTRP21
XHOH508
XHOH523
XHOH529
XHOH535
XHOH561
XHOH587
XASP44
XTYR49
XLYS78
XHIS111
XSER160
XASN161

site_idAC2
Number of Residues12
Detailsbinding site for residue UV8 X 402
ChainResidue
XTRP21
XTYR49
XTRP80
XHIS111
XPHE123
XPRO124
XARG125
XGLY129
XALA131
XLEU301
XLEU302
XNAP401

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO X 403
ChainResidue
XGLU6
XHIS201
XGLY204
XASN257
XHOH563

Functional Information from PROSITE/UniProt
site_idPS00062
Number of Residues18
DetailsALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. MeelvdeglVKALGVSNF
ChainResidueDetails
XMET145-PHE162

site_idPS00063
Number of Residues16
DetailsALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. IPKSVTpaRIvENiQV
ChainResidueDetails
XILE261-VAL276

site_idPS00798
Number of Residues18
DetailsALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRHIDCAyvyqnEheVG
ChainResidueDetails
XGLY39-GLY56

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:18087047
ChainResidueDetails
XTYR49

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:18087047
ChainResidueDetails
XTHR20
XASP44
XHIS111
XSER160
XGLN184
XTYR210
XILE261

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Lowers pKa of active site Tyr => ECO:0000250|UniProtKB:P14550
ChainResidueDetails
XLYS78

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
XARG125
XMLY263

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PDB entries from 2024-11-13

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