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2P5N

Crystal structure of mouse 17-alpha hydroxysteroid dehydrogenase in complex with coenzyme NADPH

Functional Information from GO Data
ChainGOidnamespacecontents
A0004033molecular_functionaldo-keto reductase (NADPH) activity
A0005496molecular_functionsteroid binding
A0005737cellular_componentcytoplasm
A0006694biological_processsteroid biosynthetic process
A0008202biological_processsteroid metabolic process
A0016491molecular_functionoxidoreductase activity
A0033764molecular_functionsteroid dehydrogenase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0047023molecular_functionandrosterone dehydrogenase activity
A0047024molecular_function5alpha-androstane-3beta,17beta-diol dehydrogenase activity
A0070401molecular_functionNADP+ binding
A0070402molecular_functionNADPH binding
A0072555molecular_function17-beta-ketosteroid reductase (NADPH) activity
A0072582molecular_function17-beta-hydroxysteroid dehydrogenase (NADP+) activity
A1902121molecular_functionlithocholic acid binding
B0004033molecular_functionaldo-keto reductase (NADPH) activity
B0005496molecular_functionsteroid binding
B0005737cellular_componentcytoplasm
B0006694biological_processsteroid biosynthetic process
B0008202biological_processsteroid metabolic process
B0016491molecular_functionoxidoreductase activity
B0033764molecular_functionsteroid dehydrogenase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0047023molecular_functionandrosterone dehydrogenase activity
B0047024molecular_function5alpha-androstane-3beta,17beta-diol dehydrogenase activity
B0070401molecular_functionNADP+ binding
B0070402molecular_functionNADPH binding
B0072555molecular_function17-beta-ketosteroid reductase (NADPH) activity
B0072582molecular_function17-beta-hydroxysteroid dehydrogenase (NADP+) activity
B1902121molecular_functionlithocholic acid binding
Functional Information from PDB Data
site_idAC1
Number of Residues33
DetailsBINDING SITE FOR RESIDUE NDP A 1350
ChainResidue
AGLY22
ATYR216
AGLY217
AVAL218
ALEU219
AGLY220
ATHR221
AGLN222
ATYR224
AALA253
AASN269
ATHR23
ATHR270
ASER271
ALEU272
ALYS273
AARG276
AGLU279
AASN280
AMPD1001
AHOH1354
AHOH1394
AALA24
AHOH1395
AHOH1426
AHOH1476
AHOH1556
AASP50
ATYR55
AHIS117
ASER166
AASN167
AGLN190

site_idAC2
Number of Residues35
DetailsBINDING SITE FOR RESIDUE NDP B 2350
ChainResidue
BGLY22
BTHR23
BALA24
BASP50
BTYR55
BLYS84
BHIS117
BSER166
BASN167
BGLN190
BTYR216
BGLY217
BVAL218
BLEU219
BGLY220
BTHR221
BGLN222
BTYR224
BLEU236
BALA253
BASN269
BTHR270
BSER271
BLEU272
BLYS273
BARG276
BGLU279
BASN280
BHOH2354
BHOH2391
BHOH2403
BHOH2411
BHOH2425
BHOH2426
BHOH2443

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 1001
ChainResidue
ATYR55
ATYR224
ATRP227
ANDP1350
AHOH1476

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD B 2001
ChainResidue
BTYR55
BTYR224
BTRP227
BHOH2391

Functional Information from PROSITE/UniProt
site_idPS00062
Number of Residues18
DetailsALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. MekckdaglTKSIGVSNF
ChainResidueDetails
AMET151-PHE168

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor
ChainResidueDetails
ATYR55
BTYR55

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17909281, ECO:0000269|PubMed:19237748
ChainResidueDetails
AGLY20
BGLN190
BTYR216
BTHR270
AASP50
ASER166
AGLN190
ATYR216
ATHR270
BGLY20
BASP50
BSER166

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING:
ChainResidueDetails
ALYS31
AHIS117
BLYS31
BHIS117

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Lowers pKa of active site Tyr => ECO:0000250
ChainResidueDetails
ALYS84
BLYS84

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mrq
ChainResidueDetails
ALYS84
AHIS117
AASP50
ATYR55

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mrq
ChainResidueDetails
BLYS84
BHIS117
BASP50
BTYR55

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mrq
ChainResidueDetails
ALYS84
ATYR55

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mrq
ChainResidueDetails
BLYS84
BTYR55

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PDB entries from 2024-09-18

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