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1QYV

Crystal structure of human estrogenic 17beta-hydroxysteroid dehydrogenase complex with NADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004303molecular_functionestradiol 17-beta-dehydrogenase [NAD(P)+] activity
A0005496molecular_functionsteroid binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006694biological_processsteroid biosynthetic process
A0006703biological_processestrogen biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0036094molecular_functionsmall molecule binding
A0042803molecular_functionprotein homodimerization activity
A0047035molecular_functiontestosterone dehydrogenase (NAD+) activity
A0047045molecular_functiontestosterone dehydrogenase (NADP+) activity
A0050661molecular_functionNADP binding
A0060348biological_processbone development
A0061370biological_processtestosterone biosynthetic process
A0070401molecular_functionNADP+ binding
A0071248biological_processcellular response to metal ion
A0072582molecular_function17-beta-hydroxysteroid dehydrogenase (NADP+) activity
A1903924molecular_functionestradiol binding
Functional Information from PDB Data
site_idAC1
Number of Residues31
DetailsBINDING SITE FOR RESIDUE NAP A 361
ChainResidue
AGLY9
AARG67
AASN90
AALA91
AGLY92
AVAL113
ATHR140
AGLY141
ASER142
ATYR155
ALYS159
ASER11
ACYS185
AGLY186
APRO187
AVAL188
ATHR190
AHOH602
AHOH603
AHOH619
AHOH626
AHOH662
ASER12
AHOH714
AHOH728
AGLY13
AILE14
AARG37
ALEU64
AASP65
AVAL66

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 600
ChainResidue
AARG252
AARG266
AASP269
APRO270
AHOH615
AHOH636
AHOH641

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SvgglmglpfNdvYCASKFALeGLCeSLA
ChainResidueDetails
ASER142-ALA170

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues31
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8805577","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PKA","evidences":[{"source":"PubMed","id":"8994190","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1qsg
ChainResidueDetails
AASN152
ALYS159

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1qsg
ChainResidueDetails
ATYR155
ALYS159

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PDB entries from 2025-12-17

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