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1E1Z

Crystal structure of an Arylsulfatase A mutant C69S

Functional Information from GO Data
ChainGOidnamespacecontents
P0004065molecular_functionarylsulfatase activity
P0004098molecular_functioncerebroside-sulfatase activity
P0005509molecular_functioncalcium ion binding
P0005515molecular_functionprotein binding
P0005576cellular_componentextracellular region
P0005764cellular_componentlysosome
P0005783cellular_componentendoplasmic reticulum
P0005788cellular_componentendoplasmic reticulum lumen
P0006629biological_processlipid metabolic process
P0008484molecular_functionsulfuric ester hydrolase activity
P0016787molecular_functionhydrolase activity
P0035578cellular_componentazurophil granule lumen
P0043202cellular_componentlysosomal lumen
P0046872molecular_functionmetal ion binding
P0070062cellular_componentextracellular exosome
Functional Information from PROSITE/UniProt
site_idPS00149
Number of Residues11
DetailsSULFATASE_2 Sulfatases signature 2. GYlTgmAGK.WH
ChainResidueDetails
PGLY115-HIS125

site_idPS00523
Number of Residues13
DetailsSULFATASE_1 Sulfatases signature 1. SLSTPSRaaLLTG
ChainResidueDetails
PSER67-GLY79

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:7628016
ChainResidueDetails
PSER69

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:12888274
ChainResidueDetails
PHIS125

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12888274, ECO:0007744|PDB:1N2K
ChainResidueDetails
PASP29
PASP30
PASP281
PASN282

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: via 3-oxoalanine => ECO:0000269|PubMed:12888274, ECO:0007744|PDB:1N2K
ChainResidueDetails
PSER69

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:11124905
ChainResidueDetails
PLYS123
PSER150
PHIS229
PLYS302

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: 3-oxoalanine (Cys) => ECO:0000269|PubMed:7628016, ECO:0000269|PubMed:9342345
ChainResidueDetails
PSER69

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12888274, ECO:0000269|PubMed:19159218, ECO:0007744|PDB:1N2K
ChainResidueDetails
PASN158

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12888274, ECO:0007744|PDB:1N2K
ChainResidueDetails
PASN184

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218
ChainResidueDetails
PASN350

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1auk
ChainResidueDetails
PLYS302
PHIS229
PASP281
PLYS123
PSER150
PHIS125

site_idCSA2
Number of Residues6
DetailsAnnotated By Reference To The Literature 1auk
ChainResidueDetails
PLYS302
PHIS229
PASP281
PARG73
PLYS123
PHIS125

site_idMCSA1
Number of Residues11
DetailsM-CSA 158
ChainResidueDetails

237423

PDB entries from 2025-06-11

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