1OQM
A 1:1 complex between alpha-lactalbumin and beta1,4-galactosyltransferase in the presence of UDP-N-acetyl-galactosamine
Replaces: 1L7WFunctional 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 |
| A | 0050829 | biological_process | defense response to Gram-negative bacterium |
| A | 0050830 | biological_process | defense response to Gram-positive bacterium |
| 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 |
| C | 0050829 | biological_process | defense response to Gram-negative bacterium |
| C | 0050830 | biological_process | defense response to Gram-positive bacterium |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0016757 | molecular_function | glycosyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 124 |
| Chain | Residue |
| A | LYS79 |
| A | ASP82 |
| A | GLU84 |
| A | ASP87 |
| A | ASP88 |
| A | HOH903 |
| A | HOH925 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA C 124 |
| Chain | Residue |
| C | GLU84 |
| C | ASP87 |
| C | ASP88 |
| C | HOH904 |
| C | HOH923 |
| C | LYS79 |
| C | ASP82 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 403 |
| Chain | Residue |
| B | ASP254 |
| B | MET344 |
| B | HIS347 |
| B | UD2404 |
| B | HOH989 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN D 403 |
| Chain | Residue |
| D | ASP254 |
| D | MET344 |
| D | HIS347 |
| D | UD2528 |
| D | HOH927 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE UD2 B 404 |
| Chain | Residue |
| B | PRO187 |
| B | PHE188 |
| B | ARG189 |
| B | ARG191 |
| B | PHE226 |
| B | ARG228 |
| B | ASP252 |
| B | VAL253 |
| B | ASP254 |
| B | LEU255 |
| B | MET277 |
| B | TYR289 |
| B | GLY292 |
| B | TRP314 |
| B | GLY315 |
| B | GLU317 |
| B | ASP318 |
| B | HIS347 |
| B | ASP350 |
| B | MN403 |
| B | HOH919 |
| B | HOH966 |
| B | HOH1284 |
| B | HOH1297 |
| B | HOH1465 |
| site_id | AC6 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE UD2 D 528 |
| Chain | Residue |
| D | PRO187 |
| D | PHE188 |
| D | ARG189 |
| D | ARG191 |
| D | PHE226 |
| D | ARG228 |
| D | ASP252 |
| D | VAL253 |
| D | ASP254 |
| D | LEU255 |
| D | MET277 |
| D | TYR289 |
| D | GLY291 |
| D | GLY292 |
| D | TRP314 |
| D | GLY315 |
| D | GLU317 |
| D | MET344 |
| D | HIS347 |
| D | ASP350 |
| D | ASN353 |
| D | MN403 |
| D | HOH914 |
| D | HOH927 |
| D | HOH945 |
| D | HOH965 |
| D | HOH979 |
| D | HOH1061 |
| D | HOH1105 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PG4 B 813 |
| Chain | Residue |
| B | PRO179 |
| B | HOH1264 |
| B | HOH1539 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PG4 A 814 |
| Chain | Residue |
| A | LYS114 |
| A | LEU115 |
| A | GLU116 |
| A | GLN117 |
| A | HOH1202 |
| A | HOH1506 |
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 | 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 |
