Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 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 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 | 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 |