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1FMC

7-ALPHA-HYDROXYSTEROID DEHYDROGENASE COMPLEX WITH NADH AND 7-OXO GLYCOCHENODEOXYCHOLIC ACID

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0008202biological_processsteroid metabolic process
A0008709molecular_functioncholate 7-alpha-dehydrogenase activity
A0016042biological_processlipid catabolic process
A0016491molecular_functionoxidoreductase activity
A0030573biological_processbile acid catabolic process
A0032991cellular_componentprotein-containing complex
A0042802molecular_functionidentical protein binding
A0051287molecular_functionNAD binding
A0106281molecular_functionchenodeoxycholate 7-alpha-dehydrogenase (NAD+) activity
B0005829cellular_componentcytosol
B0006629biological_processlipid metabolic process
B0008202biological_processsteroid metabolic process
B0008709molecular_functioncholate 7-alpha-dehydrogenase activity
B0016042biological_processlipid catabolic process
B0016491molecular_functionoxidoreductase activity
B0030573biological_processbile acid catabolic process
B0032991cellular_componentprotein-containing complex
B0042802molecular_functionidentical protein binding
B0051287molecular_functionNAD binding
B0106281molecular_functionchenodeoxycholate 7-alpha-dehydrogenase (NAD+) activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE CHO A 301
ChainResidue
AGLY98
ANAI302
AHOH413
AGLY99
ASER146
AALA148
AASN151
ATYR159
AALA196
ALEU197
AGLN252

site_idAC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NAI A 302
ChainResidue
AGLY18
AGLY20
AALA21
AILE23
AASP42
AILE43
ACYS67
AASP68
AILE69
AASN95
AGLY97
AILE144
ATHR145
ATYR159
ALYS163
APRO189
AGLY190
AILE192
ATHR194
AALA196
ACHO301
AHOH449
AHOH456
AHOH491

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE CHO B 301
ChainResidue
BGLY98
BGLY99
BSER146
BALA148
BASN151
BMET156
BTYR159
BGLY190
BLEU197
BGLN252
BNAI302
BHOH444
BHOH526

site_idAC4
Number of Residues26
DetailsBINDING SITE FOR RESIDUE NAI B 302
ChainResidue
BGLY18
BALA21
BGLY22
BILE23
BASP42
BILE43
BCYS67
BASP68
BILE69
BASN95
BGLY97
BILE144
BTHR145
BTYR159
BLYS163
BPRO189
BGLY190
BILE192
BTHR194
BALA196
BCHO301
BHOH404
BHOH432
BHOH446
BHOH462
BHOH502

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SmaaenkninMtsYASSKAAAsHLVrNMA
ChainResidueDetails
ASER146-ALA174

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:8672472, ECO:0000305|PubMed:9722677
ChainResidueDetails
ATYR159
BTYR159

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:8672472, ECO:0007744|PDB:1AHI, ECO:0007744|PDB:1FMC
ChainResidueDetails
AILE23
BTYR159
AGLY99
ASER146
AASN151
ATYR159
BILE23
BGLY99
BSER146
BASN151

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:8672472, ECO:0007744|PDB:1AHH, ECO:0007744|PDB:1AHI, ECO:0007744|PDB:1FMC
ChainResidueDetails
AASP42
BILE192
AASP68
AASN95
ALYS163
AILE192
BASP42
BASP68
BASN95
BLYS163

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000305|PubMed:8672472, ECO:0000305|PubMed:9722677
ChainResidueDetails
ASER146
BSER146

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Lowers pKa of active site Tyr => ECO:0000305|PubMed:8672472, ECO:0000305|PubMed:9722677
ChainResidueDetails
ALYS163
BLYS163

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PDB entries from 2024-03-27

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