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1N2K

Crystal structure of a covalent intermediate of endogenous human arylsulfatase A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004065molecular_functionarylsulfatase activity
A0004098molecular_functioncerebroside-sulfatase activity
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005764cellular_componentlysosome
A0005783cellular_componentendoplasmic reticulum
A0005788cellular_componentendoplasmic reticulum lumen
A0006629biological_processlipid metabolic process
A0008484molecular_functionsulfuric ester hydrolase activity
A0016787molecular_functionhydrolase activity
A0035578cellular_componentazurophil granule lumen
A0043202cellular_componentlysosomal lumen
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
Functional Information from PROSITE/UniProt
site_idPS00149
Number of Residues11
DetailsSULFATASE_2 Sulfatases signature 2. GYlTgmAGK.WH
ChainResidueDetails
AGLY115-HIS125

site_idPS00523
Number of Residues13
DetailsSULFATASE_1 Sulfatases signature 1. SLSTPSRaaLLTG
ChainResidueDetails
ASER67-GLY79

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"7628016","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PubMed","id":"12888274","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12888274","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1N2K","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"description":"via 3-oxoalanine","evidences":[{"source":"PubMed","id":"12888274","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1N2K","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11124905","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"3-oxoalanine (Cys)","evidences":[{"source":"PubMed","id":"7628016","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9342345","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12888274","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1N2K","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12888274","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1N2K","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1auk
ChainResidueDetails
ALYS302
AHIS229
AASP281
ALYS123
ASER150
AHIS125

site_idCSA2
Number of Residues6
DetailsAnnotated By Reference To The Literature 1auk
ChainResidueDetails
ALYS302
AHIS229
AASP281
AARG73
ALYS123
AHIS125

site_idMCSA1
Number of Residues11
DetailsM-CSA 158
ChainResidueDetails
AASP29metal ligand
ATHR286metal ligand
ATYR306electrostatic stabiliser, hydrogen bond donor
AASP30metal ligand
AFGP69electrofuge, electrophile, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, metal ligand, nucleophile, proton acceptor, proton donor, proton relay
ALEU77electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
AGLY127electrostatic stabiliser, hydrogen bond donor, increase electrophilicity
AGLY129electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AGLY154electrostatic stabiliser, hydrogen bond donor, increase electrophilicity
APHE233electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AGLU285hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor

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PDB entries from 2025-07-30

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