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2X1H

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0005739cellular_componentmitochondrion
A0005777cellular_componentperoxisome
A0006629biological_processlipid metabolic process
A0006693biological_processprostaglandin metabolic process
A0008270molecular_functionzinc ion binding
A0016491molecular_functionoxidoreductase activity
A0045599biological_processnegative regulation of fat cell differentiation
A0047522molecular_function15-oxoprostaglandin 13-reductase [NAD(P)+] activity
B0005739cellular_componentmitochondrion
B0005777cellular_componentperoxisome
B0006629biological_processlipid metabolic process
B0006693biological_processprostaglandin metabolic process
B0008270molecular_functionzinc ion binding
B0016491molecular_functionoxidoreductase activity
B0045599biological_processnegative regulation of fat cell differentiation
B0047522molecular_function15-oxoprostaglandin 13-reductase [NAD(P)+] activity
Functional Information from PDB Data
site_idAC1
Number of Residues35
DetailsBINDING SITE FOR RESIDUE NAP A 1372
ChainResidue
AASN66
ALYS200
ATYR215
ASER238
AILE260
AGLY261
APHE262
AILE263
ASER264
ATYR266
APHE294
AALA67
ALEU296
AMET347
AASN352
AX1H2001
AHOH3042
AHOH3043
AHOH3134
AHOH3161
AHOH3169
AHOH3222
ATHR150
AHOH3226
AHOH3227
AHOH3303
AHOH3312
AHOH3313
AHOH3314
AALA171
AGLY174
AGLY175
ATHR176
ACYS195
ASER196

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE X1H A 2001
ChainResidue
ASER68
AASN71
AARG76
ATYR77
APHE262
ATYR266
ATHR270
ALEU272
APHE295
ANAP1372
AHOH3315
AHOH3316
BLYS286

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE X1H A 2002
ChainResidue
ATYR152
ALEU155
ALYS156
ALEU183
ALYS186
AALA187
AMET313
AASP318
AHOH3318
BPRO269
BTHR270

site_idAC4
Number of Residues36
DetailsBINDING SITE FOR RESIDUE NAP B 1372
ChainResidue
BALA67
BTHR150
BALA171
BGLY174
BGLY175
BTHR176
BCYS195
BSER196
BLYS200
BTYR215
BSER238
BILE260
BGLY261
BPHE262
BILE263
BSER264
BTYR266
BPHE294
BLEU296
BMET347
BASN352
BEDO1362
BX1H2001
BHOH3038
BHOH3039
BHOH3103
BHOH3126
BHOH3142
BHOH3190
BHOH3256
BHOH3257
BHOH3258
BHOH3259
BHOH3260
BHOH3261
BHOH3262

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE X1H B 2001
ChainResidue
BTYR266
BTHR270
BLEU272
BPHE295
BEDO1362
BNAP1372
BHOH3194
BHOH3263
BSER68
BASN71
BARG76
BTYR77

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE X1H B 2002
ChainResidue
BALA151
BTYR152
BLEU155
BLYS156
BLEU183
BLYS186
BALA187
BHIS309
BHOH3128
BHOH3264

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 1362
ChainResidue
AGLY159
AGLY160
ALYS165
AASP233
AVAL234
AHOH3200
AHOH3217
AHOH3307
AHOH3308

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 1363
ChainResidue
APRO135
AHOH3269
AHOH3310

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1364
ChainResidue
AARG342
AASN345
ATYR346
AMET349
AHOH3311

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 1362
ChainResidue
BSER68
BVAL146
BNAP1372
BX1H2001
BHOH3040

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

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PDB entries from 2025-06-18

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