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4GQG

Crystal structure of AKR1B10 complexed with NADP+

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
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005739cellular_componentmitochondrion
A0005764cellular_componentlysosome
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0008106molecular_functionalcohol dehydrogenase (NADP+) activity
A0016488biological_processfarnesol catabolic process
A0016491molecular_functionoxidoreductase activity
A0042572biological_processretinol metabolic process
A0044597biological_processdaunorubicin metabolic process
A0044598biological_processdoxorubicin metabolic process
A0045550molecular_functiongeranylgeranyl reductase activity
A0047655molecular_functionallyl-alcohol dehydrogenase activity
A0047718molecular_functionindanol dehydrogenase activity
A0052650molecular_functionall-trans-retinol dehydrogenase (NADP+) activity
A0110095biological_processcellular detoxification of aldehyde
Functional Information from PDB Data
site_idAC1
Number of Residues35
DetailsBINDING SITE FOR RESIDUE NAP A 401
ChainResidue
AGLY19
AGLN184
ATYR210
ASER211
APRO212
ALEU213
AGLY214
ASER215
APRO216
AASP217
AALA246
ATHR20
AILE261
APRO262
ALYS263
ASER264
AVAL265
ATHR266
AARG269
AGLU272
AASN273
AHOH537
ATRP21
AHOH560
AHOH568
AHOH581
AHOH582
AHOH624
AHOH764
ALYS22
AASP44
ATYR49
AHIS111
ASER160
AASN161

Functional Information from PROSITE/UniProt
site_idPS00062
Number of Residues18
DetailsALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. MeelvdeglVKALGVSNF
ChainResidueDetails
AMET145-PHE162

site_idPS00063
Number of Residues16
DetailsALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. IPKSVTpaRIvENiQV
ChainResidueDetails
AILE261-VAL276

site_idPS00798
Number of Residues18
DetailsALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRHIDCAyvyqnEheVG
ChainResidueDetails
AGLY39-GLY56

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:18087047
ChainResidueDetails
ATYR49

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:18087047
ChainResidueDetails
AASP44
AHIS111
ASER160
AGLN184
ATYR210
AILE261
ATHR20

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Lowers pKa of active site Tyr => ECO:0000250|UniProtKB:P14550
ChainResidueDetails
ALYS78

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS263
ALYS125

218500

PDB entries from 2024-04-17

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