1AUK
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 PDB Data
| site_id | ACT |
| Number of Residues | 1 |
| Details | RESIDUE 69 WAS TREATED AS A GLYCINE DURING REFINEMENT TO AVOID BIAS IN THE INTERPRETATION OF THE DIFFERENCE ELECTRON DENSITY MAP. THE SIDE CHAIN OF RESIDUE 69 WAS INTERPRETED AS AN ALDEHYDE GROUP WITH TWO-FOLD DISORDERED ALDEHYDE FUNCTION (I.E. THE CARBONYL OXYGEN ATOM OCCUPIES TWO DIFFERENT POSITIONS). THE AUTHORS ASSUME THAT THE ALDEHYDE IS IN EQUILIBRIUM WITH ITS HYDRATED FORM, THE GEMINAL DIOL, WHICH IS IN ACCORDANCE WITH THE SHAPE OF THE ELECTRON DENSITY. |
| Chain | Residue |
| A | FGL69 |
Functional Information from PROSITE/UniProt
| site_id | PS00149 |
| Number of Residues | 11 |
| Details | SULFATASE_2 Sulfatases signature 2. GYlTgmAGK.WH |
| Chain | Residue | Details |
| A | GLY115-HIS125 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:7628016 |
| Chain | Residue | Details |
| A | FGL69 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:12888274 |
| Chain | Residue | Details |
| A | HIS125 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12888274, ECO:0007744|PDB:1N2K |
| Chain | Residue | Details |
| A | ASP29 | |
| A | ASP30 | |
| A | ASP281 | |
| A | ASN282 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: via 3-oxoalanine => ECO:0000269|PubMed:12888274, ECO:0007744|PDB:1N2K |
| Chain | Residue | Details |
| A | FGL69 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11124905 |
| Chain | Residue | Details |
| A | LYS123 | |
| A | SER150 | |
| A | HIS229 | |
| A | LYS302 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: 3-oxoalanine (Cys) => ECO:0000269|PubMed:7628016, ECO:0000269|PubMed:9342345 |
| Chain | Residue | Details |
| A | FGL69 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12888274, ECO:0000269|PubMed:19159218, ECO:0007744|PDB:1N2K |
| Chain | Residue | Details |
| A | ASN158 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12888274, ECO:0007744|PDB:1N2K |
| Chain | Residue | Details |
| A | ASN184 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 |
| Chain | Residue | Details |
| A | ASN350 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | a catalytic site defined by CSA, PubMed 11124905, 17558559, 9521684 |
| Chain | Residue | Details |
| A | ASP281 | |
| A | HIS125 | |
| A | HIS229 | |
| A | LYS123 | |
| A | SER150 | |
| A | LYS302 |
| 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 | FGL69 | 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 |
