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1BHS

HUMAN ESTROGENIC 17BETA-HYDROXYSTEROID DEHYDROGENASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
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
A0007040biological_processlysosome organization
A0007519biological_processskeletal muscle tissue development
A0008210biological_processestrogen metabolic process
A0010467biological_processgene expression
A0016491molecular_functionoxidoreductase activity
A0030283molecular_functiontestosterone dehydrogenase [NAD(P)+] activity
A0035410molecular_functionobsolete dihydrotestosterone 17-beta-dehydrogenase activity
A0036094molecular_functionsmall molecule binding
A0042803molecular_functionprotein homodimerization activity
A0047035molecular_functiontestosterone dehydrogenase (NAD+) activity
A0047045molecular_functiontestosterone 17-beta-dehydrogenase (NADP+) activity
A0050661molecular_functionNADP binding
A0060348biological_processbone development
A0060612biological_processadipose tissue 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_idCAT
Number of Residues3
DetailsTHE TYR-LYS-SER CATALYTIC TRIAD.
ChainResidue
ATYR155
ALYS159
ASER142

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
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
ACYS156

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:8805577
ChainResidueDetails
ACYS10
AVAL66
AVAL143
APHE160

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:8994190
ChainResidueDetails
AGLY135

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

226707

PDB entries from 2024-10-30

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