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2C0C

Structure of the MGC45594 gene product

Functional Information from GO Data
ChainGOidnamespacecontents
A0003674molecular_functionmolecular_function
A0005777cellular_componentperoxisome
A0006629biological_processlipid metabolic process
A0006693biological_processprostaglandin metabolic process
A0008150biological_processbiological_process
A0008270molecular_functionzinc ion binding
A0016491molecular_functionoxidoreductase activity
A0036132molecular_function13-prostaglandin reductase activity
A0045599biological_processnegative regulation of fat cell differentiation
A0047522molecular_function15-oxoprostaglandin 13-oxidase activity
B0003674molecular_functionmolecular_function
B0005777cellular_componentperoxisome
B0006629biological_processlipid metabolic process
B0006693biological_processprostaglandin metabolic process
B0008150biological_processbiological_process
B0008270molecular_functionzinc ion binding
B0016491molecular_functionoxidoreductase activity
B0036132molecular_function13-prostaglandin reductase activity
B0045599biological_processnegative regulation of fat cell differentiation
B0047522molecular_function15-oxoprostaglandin 13-oxidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues36
DetailsBINDING SITE FOR RESIDUE NAP A1363
ChainResidue
AASN66
ALYS200
ATYR215
ASER238
AILE260
AGLY261
APHE262
AILE263
ASER264
ATYR266
APHE294
AALA67
ALEU296
AMET347
AASN352
AHOH2073
AHOH2075
AHOH2174
AHOH2188
AHOH2195
AHOH2254
AHOH2258
ATHR150
AHOH2348
AHOH2349
AHOH2350
AHOH2351
AHOH2352
AHOH2353
AHOH2354
AALA171
AGLY174
AGLY175
ATHR176
ACYS195
ASER196

site_idAC2
Number of Residues38
DetailsBINDING SITE FOR RESIDUE NAP B1363
ChainResidue
BASN66
BALA67
BTHR150
BALA171
BGLY174
BGLY175
BTHR176
BCYS195
BSER196
BLYS200
BTYR215
BSER238
BVAL239
BILE260
BGLY261
BPHE262
BILE263
BSER264
BTYR266
BPHE294
BLEU296
BMET347
BTYR348
BASN352
BHOH2074
BHOH2075
BHOH2155
BHOH2226
BHOH2309
BHOH2312
BHOH2313
BHOH2314
BHOH2315
BHOH2316
BHOH2317
BHOH2318
BHOH2319
BHOH2320

Functional Information from PROSITE/UniProt
site_idPS01162
Number of Residues22
DetailsQOR_ZETA_CRYSTAL Quinone oxidoreductase / zeta-crystallin signature. GKkvLvtaAAGGtGqfamQlsK
ChainResidueDetails
AGLY164-LYS185

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|Ref.9
ChainResidueDetails
ATHR176
BTHR176
BSER196
BLYS200
BTYR215
BSER238
BILE260
BTYR266
BPHE294
BASN352
ASER196
ALYS200
ATYR215
ASER238
AILE260
ATYR266
APHE294
AASN352

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q8BGC4
ChainResidueDetails
ALYS26
BLYS26

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER290
BSER290

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1guf
ChainResidueDetails
ATYR77

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1guf
ChainResidueDetails
BTYR77

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1guf
ChainResidueDetails
ASER68
AASN71

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1guf
ChainResidueDetails
BSER68
BASN71

223166

PDB entries from 2024-07-31

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