1N2K
Crystal structure of a covalent intermediate of endogenous human arylsulfatase A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004065 | molecular_function | arylsulfatase activity |
| A | 0004098 | molecular_function | cerebroside-sulfatase activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005764 | cellular_component | lysosome |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005788 | cellular_component | endoplasmic reticulum lumen |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0008484 | molecular_function | sulfuric ester hydrolase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0035578 | cellular_component | azurophil granule lumen |
| A | 0043202 | cellular_component | lysosomal lumen |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070062 | cellular_component | extracellular exosome |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"7628016","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"12888274","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12888274","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1N2K","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"via 3-oxoalanine","evidences":[{"source":"PubMed","id":"12888274","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1N2K","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11124905","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"3-oxoalanine (Cys)","evidences":[{"source":"PubMed","id":"7628016","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9342345","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Glycosylation: {"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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12888274","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1N2K","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1auk |
| Chain | Residue | Details |
| A | LYS302 | |
| A | HIS229 | |
| A | ASP281 | |
| A | LYS123 | |
| A | SER150 | |
| A | HIS125 |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1auk |
| Chain | Residue | Details |
| A | LYS302 | |
| A | HIS229 | |
| A | ASP281 | |
| A | ARG73 | |
| A | LYS123 | |
| A | HIS125 |
| site_id | MCSA1 |
| Number of Residues | 11 |
| Details | M-CSA 158 |
| Chain | Residue | Details |
| A | ASP29 | metal ligand |
| A | THR286 | metal ligand |
| A | TYR306 | electrostatic stabiliser, hydrogen bond donor |
| A | ASP30 | metal ligand |
| A | FGP69 | electrofuge, electrophile, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, metal ligand, nucleophile, proton acceptor, proton donor, proton relay |
| A | LEU77 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| A | GLY127 | electrostatic stabiliser, hydrogen bond donor, increase electrophilicity |
| A | GLY129 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLY154 | electrostatic stabiliser, hydrogen bond donor, increase electrophilicity |
| A | PHE233 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLU285 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
