1NQI
crystal structure of lactose synthase, a 1:1 complex between beta1,4-galactosyltransferase and alpha-lactalbumin in the presence of GlcNAc
Replaces: 1J92Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003796 | molecular_function | lysozyme activity |
| A | 0004461 | molecular_function | lactose synthase activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005989 | biological_process | lactose biosynthetic process |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| C | 0003796 | molecular_function | lysozyme activity |
| C | 0004461 | molecular_function | lactose synthase activity |
| C | 0005509 | molecular_function | calcium ion binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005576 | cellular_component | extracellular region |
| C | 0005989 | biological_process | lactose biosynthetic process |
| C | 0032991 | cellular_component | protein-containing complex |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0016757 | molecular_function | glycosyltransferase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00128 |
| Number of Residues | 19 |
| Details | GLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. CgisCdkLlddELdddiaC |
| Chain | Residue | Details |
| A | CYS73-CYS91 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: |
| Chain | Residue | Details |
| B | PRO187 | |
| D | PHE226 | |
| D | VAL253 | |
| D | ASP254 | |
| D | TRP314 | |
| D | GLY316 | |
| D | HIS347 | |
| D | ARG359 | |
| B | PHE226 | |
| B | VAL253 | |
| B | ASP254 | |
| B | TRP314 | |
| B | GLY316 | |
| B | HIS347 | |
| B | ARG359 | |
| D | PRO187 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN45 | |
| C | ASN45 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1fr8 |
| Chain | Residue | Details |
| B | ARG359 | |
| B | GLU317 | |
| B | ASP319 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1fr8 |
| Chain | Residue | Details |
| D | ARG359 | |
| D | GLU317 | |
| D | ASP319 |
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 570 |
| Chain | Residue | Details |
| B | ASP252 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| B | ASP254 | metal ligand |
| B | TRP314 | electrostatic stabiliser, hydrogen bond donor |
| B | GLU317 | electrostatic stabiliser, hydrogen bond acceptor |
| B | ASP318 | activator, electrostatic stabiliser, proton acceptor, proton donor |
| B | MET344 | metal ligand |
| B | HIS347 | metal ligand |
| B | ARG349 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 8 |
| Details | M-CSA 570 |
| Chain | Residue | Details |
| D | ASP252 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| D | ASP254 | metal ligand |
| D | TRP314 | electrostatic stabiliser, hydrogen bond donor |
| D | GLU317 | electrostatic stabiliser, hydrogen bond acceptor |
| D | ASP318 | activator, electrostatic stabiliser, proton acceptor, proton donor |
| D | MET344 | metal ligand |
| D | HIS347 | metal ligand |
| D | ARG349 | electrostatic stabiliser, hydrogen bond donor |
