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1WMA

Crystal structure of human CBR1 in complex with Hydroxy-PP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004090molecular_functioncarbonyl reductase (NADPH) activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006805biological_processxenobiotic metabolic process
A0008106molecular_functionalcohol dehydrogenase (NADP+) activity
A0008211biological_processglucocorticoid metabolic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0016655molecular_functionoxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor
A0019371biological_processcyclooxygenase pathway
A0030855biological_processepithelial cell differentiation
A0042373biological_processvitamin K metabolic process
A0047020molecular_function15-hydroxyprostaglandin-D dehydrogenase (NADP+) activity
A0047021molecular_function15-hydroxyprostaglandin dehydrogenase (NADP+) activity
A0050221molecular_functionprostaglandin E2 9-reductase activity
A0070062cellular_componentextracellular exosome
A0160163molecular_functionS-nitrosoglutathione reductase (NADPH) activity
A1903561cellular_componentextracellular vesicle
A2000379biological_processpositive regulation of reactive oxygen species metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 300
ChainResidue
AARG57
APHE58
AHOH542
AHOH639

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
ASO4305
AHOH424
AHOH458
AHOH553
AHOH559
APHE102
ASER190
ASER191
AALA192
ATYR193

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
ALYS216
AGLY217
AASP218
ALYS219
AHOH506
AHOH511
AHOH761

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 303
ChainResidue
AASP64
ALYS111
ATHR163
AARG209
ALYS210
AGLU213
AHOH446
AHOH460
AHOH677

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 304
ChainResidue
AARG41
AARG118
AHOH571
AHOH656
AHOH675
AHOH684

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 305
ChainResidue
AVAL96
AALA97
AARG272
ASO4301
AHOH502
AHOH553
AHOH559
AHOH576

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 306
ChainResidue
ASER2
AGLY3
AGLN47
AGLN50
ALYS129
AHOH742

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE AB3 A 307
ChainResidue
ASER139
AMET141
ATYR193
AGLY228
ATRP229
AAB3308
ANDP309
APE5310
AHOH479

site_idAC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE AB3 A 308
ChainResidue
AARG22
AARG26
AILE140
AARG144
AGLU244
AAB3307
APE5310
AHOH484
AHOH607
AHOH642

site_idBC1
Number of Residues39
DetailsBINDING SITE FOR RESIDUE NDP A 309
ChainResidue
AHOH430
AHOH449
AHOH481
AHOH523
AHOH549
AHOH661
AHOH664
AHOH666
AHOH721
AGLY11
AASN13
ALYS14
AGLY15
AILE16
AARG37
ALEU61
AASP62
AILE63
AASP64
AASN89
AALA90
AGLY91
AILE92
AVAL137
ASER138
ATYR193
ALYS197
APRO227
AGLY228
ATRP229
AVAL230
ATHR232
AASP233
AMET234
AALA235
AAB3307
AHOH402
AHOH406
AHOH407

site_idBC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PE5 A 310
ChainResidue
AASP23
AALA93
AMET141
AARG144
AMET234
AGLU248
ATYR252
AAB3307
AAB3308
AHOH416
AHOH423
AHOH466
AHOH495

site_idBC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE P33 A 311
ChainResidue
AALA93
ATHR122
ALEU125
AHIS207
ALYS210
ALEU211
AGLN214
AHOH623
AHOH697
AHOH730

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. KgvhqkegwpSsaYGVTKIGVtVLSrIHA
ChainResidueDetails
ALYS180-ALA208

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AGLY194

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:15799708, ECO:0000269|PubMed:17912391, ECO:0000269|PubMed:18826943
ChainResidueDetails
ATHR10
AILE63
AALA90
AGLY194
AARG231

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING:
ChainResidueDetails
ALYS95
AALA106
AILE140
ATYR193

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P47727
ChainResidueDetails
ASER2

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P48758
ChainResidueDetails
AGLY30

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-1-carboxyethyl lysine => ECO:0000269|PubMed:8421682
ChainResidueDetails
AALA239

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
AGLU152
ATYR193
ASER139
ALYS197

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
AASN113
ATYR193
ASER139
ALYS197

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
ALYS197
ASER190

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
ATYR193
ALYS197

226707

PDB entries from 2024-10-30

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