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1P49

Structure of Human Placental Estrone/DHEA Sulfatase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004065molecular_functionarylsulfatase activity
A0004773molecular_functionsteryl-sulfatase activity
A0005764cellular_componentlysosome
A0005768cellular_componentendosome
A0005783cellular_componentendoplasmic reticulum
A0005788cellular_componentendoplasmic reticulum lumen
A0005789cellular_componentendoplasmic reticulum membrane
A0005794cellular_componentGolgi apparatus
A0005886cellular_componentplasma membrane
A0006706biological_processsteroid catabolic process
A0007565biological_processfemale pregnancy
A0008202biological_processsteroid metabolic process
A0008484molecular_functionsulfuric ester hydrolase activity
A0008544biological_processepidermis development
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0031410cellular_componentcytoplasmic vesicle
A0033163cellular_componentmicroneme membrane
A0043231cellular_componentintracellular membrane-bounded organelle
A0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00149
Number of Residues11
DetailsSULFATASE_2 Sulfatases signature 2. GYsTalIGK.WH
ChainResidueDetails
AGLY126-HIS136

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues510
DetailsTOPO_DOM: Lumenal => ECO:0000269|PubMed:2668275
ChainResidueDetails
AHIS22-ARG184
AHIS235-ARG583

site_idSWS_FT_FI2
Number of Residues44
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:2668275
ChainResidueDetails
ALEU185-LEU208
ALEU213-LEU234

site_idSWS_FT_FI3
Number of Residues3
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:2668275
ChainResidueDetails
ALEU209-PRO212

site_idSWS_FT_FI4
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:12657638
ChainResidueDetails
AALS75

site_idSWS_FT_FI5
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:12657638
ChainResidueDetails
AHIS136

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12657638
ChainResidueDetails
AASP35
AASP36
AASP342
AGLN343

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: via 3-oxoalanine => ECO:0000269|PubMed:12657638
ChainResidueDetails
AALS75

site_idSWS_FT_FI8
Number of Residues2
DetailsSITE: Not glycosylated => ECO:0000269|PubMed:2668275
ChainResidueDetails
AASN333
AASN459

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: 3-oxoalanine (Cys) => ECO:0000269|PubMed:12657638
ChainResidueDetails
AALS75

site_idSWS_FT_FI10
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12657638, ECO:0000269|PubMed:2668275
ChainResidueDetails
AASN47
AASN259

222926

PDB entries from 2024-07-24

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