1O23
CRYSTAL STRUCTURE OF LACTOSE SYNTHASE IN THE PRESENCE OF UDP-GLUCOSE
Replaces: 1NT7Replaces: 1JNCFunctional 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 | HOH903 |
| A | HOH912 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA C 806 |
| Chain | Residue |
| C | GLU486 |
| C | ASP489 |
| C | ASP490 |
| C | HOH911 |
| C | HOH944 |
| C | LYS481 |
| C | ASP484 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 807 |
| Chain | Residue |
| B | ASP254 |
| B | MET344 |
| B | HIS347 |
| B | UPG809 |
| B | HOH919 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN D 808 |
| Chain | Residue |
| D | ASP656 |
| D | MET746 |
| D | HIS749 |
| D | UPG810 |
| D | HOH907 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE UPG B 809 |
| Chain | Residue |
| B | PRO187 |
| B | PHE188 |
| B | ARG189 |
| B | ARG191 |
| B | PHE226 |
| B | ARG228 |
| B | ASP252 |
| B | VAL253 |
| B | ASP254 |
| B | TYR289 |
| B | GLY292 |
| B | TRP314 |
| B | GLU317 |
| B | ASP318 |
| B | MET344 |
| B | HIS347 |
| B | ASP350 |
| B | MN807 |
| B | HOH919 |
| B | HOH960 |
| B | HOH962 |
| B | HOH1017 |
| B | HOH1034 |
| B | HOH1060 |
| B | HOH1081 |
| site_id | AC6 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE UPG D 810 |
| Chain | Residue |
| D | PRO589 |
| D | PHE590 |
| D | ARG591 |
| D | ARG593 |
| D | PHE628 |
| D | ARG630 |
| D | ASP654 |
| D | VAL655 |
| D | ASP656 |
| D | TYR691 |
| D | GLY694 |
| D | TRP716 |
| D | GLY717 |
| D | GLU719 |
| D | ASP720 |
| D | MET746 |
| D | HIS749 |
| D | ASP752 |
| D | MN808 |
| D | HOH907 |
| D | HOH909 |
| D | HOH1002 |
| D | HOH1135 |
| D | HOH1198 |
| D | HOH1203 |
| site_id | AC7 |
| 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 | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE UDP D 812 |
| Chain | Residue |
| D | LEU557 |
| D | LYS558 |
| D | TYR790 |
| D | PRO791 |
| D | LEU792 |
| D | TYR793 |
| D | LYS795 |
| D | HOH1098 |
| D | HOH1182 |
| D | HOH1233 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PG4 A 813 |
| Chain | Residue |
| A | GLY35 |
| A | ALA40 |
| A | HOH950 |
| A | HOH1271 |
| B | LYS279 |
| B | TRP314 |
| B | ARG349 |
| A | GLU2 |
| A | PHE31 |
| A | HIS32 |
| A | THR33 |
| A | SER34 |
| site_id | BC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PG4 C 814 |
| Chain | Residue |
| C | PHE433 |
| C | HIS434 |
| C | THR435 |
| C | SER436 |
| C | GLY437 |
| C | HOH926 |
| C | HOH1030 |
| C | HOH1330 |
| D | PHE682 |
| D | TRP716 |
| D | ARG751 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MES A 815 |
| Chain | Residue |
| A | LYS114 |
| A | LEU115 |
| A | GLU116 |
| A | HOH948 |
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 | VAL253 | |
| B | ASP254 | |
| B | TRP314 | |
| B | GLY316 | |
| B | HIS347 | |
| B | ARG359 | |
| D | PRO589 | |
| D | PHE628 | |
| D | VAL655 | |
| D | ASP656 | |
| D | TRP716 | |
| D | GLY718 | |
| D | HIS749 | |
| D | ARG761 | |
| B | PRO187 | |
| B | PHE226 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN45 | |
| C | ASN447 |
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 | TRP716 | electrostatic stabiliser, hydrogen bond donor |
| D | GLU719 | electrostatic stabiliser, hydrogen bond acceptor |
| D | ASP654 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| D | ASP656 | metal ligand |
| D | ASP720 | activator, electrostatic stabiliser, proton acceptor, proton donor |
| D | MET746 | metal ligand |
| D | HIS749 | metal ligand |
| D | ARG751 | electrostatic stabiliser, hydrogen bond donor |
