Functional 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 805 |
| Chain | Residue |
| A | LYS79 |
| A | ASP82 |
| A | GLU84 |
| A | ASP87 |
| A | ASP88 |
| A | HOH909 |
| A | HOH945 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA C 806 |
| Chain | Residue |
| C | GLU84 |
| C | ASP87 |
| C | ASP88 |
| C | HOH910 |
| C | HOH922 |
| C | LYS79 |
| C | ASP82 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 807 |
| Chain | Residue |
| B | ASP254 |
| B | MET344 |
| B | HIS347 |
| B | UDP809 |
| B | HOH908 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN D 808 |
| Chain | Residue |
| D | ASP254 |
| D | MET344 |
| D | HIS347 |
| D | UDP810 |
| D | HOH902 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 818 |
| Chain | Residue |
| D | GLU148 |
| D | PHE149 |
| D | ASN150 |
| D | ARG343 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 819 |
| Chain | Residue |
| A | THR4 |
| A | LYS7 |
| A | HOH1077 |
| A | HOH1288 |
| site_id | AC7 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE UDP B 809 |
| Chain | Residue |
| B | PRO187 |
| B | PHE188 |
| B | ARG189 |
| B | ARG191 |
| B | PHE226 |
| B | ASP252 |
| B | VAL253 |
| B | ASP254 |
| B | TRP314 |
| B | MET344 |
| B | HIS347 |
| B | ASP350 |
| B | MN807 |
| B | PG4817 |
| B | HOH908 |
| B | HOH912 |
| B | HOH937 |
| B | HOH959 |
| B | HOH976 |
| B | HOH992 |
| B | HOH1026 |
| B | HOH1210 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE UDP D 810 |
| Chain | Residue |
| D | PRO187 |
| D | PHE188 |
| D | ARG189 |
| D | ARG191 |
| D | PHE226 |
| D | ASP252 |
| D | VAL253 |
| D | ASP254 |
| D | TRP314 |
| D | MET344 |
| D | HIS347 |
| D | ARG349 |
| D | ASP350 |
| D | MN808 |
| D | PG4816 |
| D | HOH902 |
| D | HOH919 |
| D | HOH925 |
| D | HOH931 |
| D | HOH1018 |
| D | HOH1181 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE UDP B 811 |
| Chain | Residue |
| B | LEU155 |
| B | LYS156 |
| B | GLU159 |
| B | GLN192 |
| B | GLN386 |
| B | TYR388 |
| B | PRO389 |
| B | LEU390 |
| B | TYR391 |
| B | LYS393 |
| site_id | BC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE UDP D 812 |
| Chain | Residue |
| D | LEU155 |
| D | LYS156 |
| D | GLU159 |
| D | GLN386 |
| D | TYR388 |
| D | PRO389 |
| D | LEU390 |
| D | TYR391 |
| D | HOH958 |
| D | HOH1285 |
| D | HOH1301 |
| D | HOH1331 |
| site_id | BC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PG4 A 813 |
| Chain | Residue |
| A | HIS32 |
| A | SER34 |
| A | GLY35 |
| A | ALA40 |
| A | HOH940 |
| A | HOH1279 |
| B | LYS279 |
| B | TRP314 |
| B | ARG349 |
| B | PG4817 |
| A | GLU2 |
| A | PHE31 |
| site_id | BC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PG4 C 814 |
| Chain | Residue |
| C | PHE31 |
| C | HIS32 |
| C | THR33 |
| C | SER34 |
| C | GLY35 |
| C | ASP37 |
| C | ALA40 |
| C | HOH967 |
| C | HOH1183 |
| D | TRP314 |
| D | ARG359 |
| D | PG4816 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PG4 B 815 |
| Chain | Residue |
| B | ASP242 |
| B | VAL385 |
| B | ARG387 |
| B | HOH1107 |
| B | HOH1287 |
| B | HOH1495 |
| D | ARG387 |
| site_id | BC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PG4 D 816 |
| Chain | Residue |
| C | PHE31 |
| C | PG4814 |
| D | LYS279 |
| D | PHE280 |
| D | TYR286 |
| D | TYR289 |
| D | GLY292 |
| D | TRP314 |
| D | ASP318 |
| D | UDP810 |
| D | HOH1132 |
| D | HOH1159 |
| D | HOH1181 |
| D | HOH1281 |
| site_id | BC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PG4 B 817 |
| Chain | Residue |
| A | PHE31 |
| A | PG4813 |
| B | LYS279 |
| B | PHE280 |
| B | TYR286 |
| B | TRP314 |
| B | GLY316 |
| B | ASP318 |
| B | ASP319 |
| B | UDP809 |
| B | HOH912 |
| B | HOH1026 |
| B | HOH1190 |
| B | HOH1240 |
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 |
