Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2WEK

Crystal structure of the human MGC45594 gene product in complex with diclofenac

Functional Information from GO Data
ChainGOidnamespacecontents
A0005739cellular_componentmitochondrion
A0005777cellular_componentperoxisome
A0006629biological_processlipid metabolic process
A0008270molecular_functionzinc ion binding
A0016491molecular_functionoxidoreductase activity
A0045599biological_processnegative regulation of fat cell differentiation
A0047522molecular_function15-oxoprostaglandin 13-oxidase [NAD(P)+] activity
B0005739cellular_componentmitochondrion
B0005777cellular_componentperoxisome
B0006629biological_processlipid metabolic process
B0008270molecular_functionzinc ion binding
B0016491molecular_functionoxidoreductase activity
B0045599biological_processnegative regulation of fat cell differentiation
B0047522molecular_function15-oxoprostaglandin 13-oxidase [NAD(P)+] activity
Functional Information from PDB Data
site_idAC1
Number of Residues37
DetailsBINDING SITE FOR RESIDUE NAP A 1372
ChainResidue
AASN75
ALYS209
ATYR224
ASER247
AVAL248
AILE269
AGLY270
APHE271
AILE272
ASER273
ATYR275
AALA76
APHE303
ALEU305
AMET356
AGLY359
AASN361
ADIF1373
AGOL1379
AHOH2025
AHOH2027
AHOH2088
ATHR159
AHOH2105
AHOH2159
AHOH2210
AHOH2211
AHOH2212
AHOH2213
AHOH2214
AHOH2215
AALA180
AGLY183
AGLY184
ATHR185
ACYS204
ASER205

site_idAC2
Number of Residues37
DetailsBINDING SITE FOR RESIDUE NAP B 1372
ChainResidue
BASN75
BALA76
BTHR159
BALA180
BGLY183
BGLY184
BTHR185
BCYS204
BSER205
BLYS209
BTYR224
BSER247
BILE269
BGLY270
BPHE271
BILE272
BSER273
BTYR275
BPHE303
BLEU305
BMET356
BTYR357
BASN361
BDIF1373
BDIF1376
BGOL1378
BHOH2013
BHOH2014
BHOH2052
BHOH2064
BHOH2105
BHOH2156
BHOH2161
BHOH2162
BHOH2163
BHOH2164
BHOH2165

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE DIF A 1373
ChainResidue
ASER77
APHE98
AMET124
AVAL155
ATYR275
APHE304
AASN306
ANAP1372
ADIF1374
AHOH2216

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE DIF B 1373
ChainResidue
BSER77
BPHE98
BMET124
BVAL155
BTYR275
BPHE304
BASN306
BNAP1372
BDIF1374
BHOH2167

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE DIF B 1374
ChainResidue
BASN306
BLEU309
BDIF1373
BTYR86
BPHE98
BMET124
BPRO126
BILE139

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DIF B 1375
ChainResidue
BTYR161
BLYS165
BLEU192
BLYS195
BHIS318
BHOH2168
BHOH2169

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE DIF A 1374
ChainResidue
ATYR86
APHE98
AMET124
APRO126
AASN306
ADIF1373

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE DIF A 1375
ChainResidue
ASER138
AILE139
ALEU309
ATYR312
AGLN313
AHOH2217

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE DIF B 1376
ChainResidue
BTYR224
BGLY249
BALA251
BMET252
BSER273
BNAP1372

site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE DIF A 1376
ChainResidue
ATYR161
ALYS165
ALEU192
ALYS195
AHIS318
AMET322
AHOH2091
AHOH2218
BPRO283

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 B 1377
ChainResidue
BPRO43
BASN44
BPHE45
BILE79
BGLN276
BASN354
BHOH2170

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 1377
ChainResidue
APRO43
AASN44
APHE45
AILE79
AGLN276
AHOH2011

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 1378
ChainResidue
BTYR224
BLYS225
BTYR357
BGLY359
BNAP1372

site_idBC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1379
ChainResidue
ASER205
ATYR224
ALYS225
AMET358
AGLY359
ANAP1372
AHOH2124

site_idBC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 1379
ChainResidue
BPRO238
BASP258
BLYS296
BHOH2103
BHOH2171
BHOH2172
BHOH2173

site_idBC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 1380
ChainResidue
AASN80
AARG85
APHE271
ATYR275
ATHR279
AGLY280
AGOL1381
AHOH2220

site_idBC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1381
ChainResidue
AARG85
APHE304
AGOL1380
AHOH2219
AHOH2220
BLEU294
BLYS295

Functional Information from PROSITE/UniProt
site_idPS01162
Number of Residues22
DetailsQOR_ZETA_CRYSTAL Quinone oxidoreductase / zeta-crystallin signature. GKkvLvtaAAGGtGqfamQlsK
ChainResidueDetails
AGLY173-LYS194

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|Ref.9
ChainResidueDetails
ATHR185
BTHR185
BSER205
BLYS209
BTYR224
BSER247
BILE269
BTYR275
BPHE303
BASN361
ASER205
ALYS209
ATYR224
ASER247
AILE269
ATYR275
APHE303
AASN361

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q8BGC4
ChainResidueDetails
ALYS35
BLYS35

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER299
BSER299

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1guf
ChainResidueDetails
ATYR86

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1guf
ChainResidueDetails
BTYR86

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1guf
ChainResidueDetails
AASN80
ASER77

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1guf
ChainResidueDetails
BASN80
BSER77

231029

PDB entries from 2025-02-05

PDB statisticsPDBj update infoContact PDBjnumon