2FYC
Crystal structure of the catalytic domain of bovine beta1,4-galactosyltransferase-I in complex with alpha-lactalbumin, Ca and UDP-galactose
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 | 27 |
| Details | BINDING SITE FOR RESIDUE GDU B 403 |
| Chain | Residue |
| B | PRO187 |
| B | LYS279 |
| B | GLY292 |
| B | TRP314 |
| B | GLY315 |
| B | GLU317 |
| B | ASP318 |
| B | HIS347 |
| B | ASP350 |
| B | CA404 |
| B | HOH1018 |
| B | PHE188 |
| B | HOH1027 |
| B | HOH1032 |
| B | HOH1114 |
| B | HOH1158 |
| B | HOH1267 |
| B | HOH1394 |
| B | HOH1556 |
| B | HOH1641 |
| B | ARG189 |
| B | ARG191 |
| B | PHE226 |
| B | ARG228 |
| B | ASP252 |
| B | VAL253 |
| B | ASP254 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE GDU D 528 |
| Chain | Residue |
| D | PRO187 |
| D | PHE188 |
| D | ARG189 |
| D | ARG191 |
| D | PHE226 |
| D | ARG228 |
| D | ASP252 |
| D | VAL253 |
| D | ASP254 |
| D | LYS279 |
| D | GLY292 |
| D | TRP314 |
| D | GLY315 |
| D | GLU317 |
| D | ASP318 |
| D | HIS347 |
| D | ASP350 |
| D | ASN353 |
| D | CA527 |
| D | HOH1028 |
| D | HOH1039 |
| D | HOH1040 |
| D | HOH1084 |
| D | HOH1093 |
| D | HOH1126 |
| D | HOH1555 |
| site_id | AC3 |
| 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 | HOH1005 |
| A | HOH1014 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA C 526 |
| Chain | Residue |
| C | LYS79 |
| C | ASP82 |
| C | GLU84 |
| C | ASP87 |
| C | ASP88 |
| C | HOH1006 |
| C | HOH1057 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 404 |
| Chain | Residue |
| B | ASP254 |
| B | HIS344 |
| B | HIS347 |
| B | GDU403 |
| B | HOH1027 |
| B | HOH1158 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA D 527 |
| Chain | Residue |
| D | ASP254 |
| D | HIS344 |
| D | HIS347 |
| D | GDU528 |
| D | HOH1028 |
| D | HOH1093 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE UDP B 405 |
| Chain | Residue |
| B | LEU155 |
| B | GLU159 |
| B | GLN192 |
| B | GLN386 |
| B | TYR388 |
| B | PRO389 |
| B | LEU390 |
| B | TYR391 |
| B | LYS393 |
| B | HOH1180 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE UDP D 529 |
| Chain | Residue |
| D | HOH1133 |
| D | HOH1659 |
| D | LEU155 |
| D | LYS156 |
| D | GLU159 |
| D | GLN192 |
| D | GLN386 |
| D | TYR388 |
| D | PRO389 |
| D | LEU390 |
| D | TYR391 |
| D | LYS393 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MES A 805 |
| Chain | Residue |
| A | GLU49 |
| A | GLN54 |
| A | LYS99 |
| A | TYR103 |
| A | LYS105 |
| A | HOH1038 |
| A | HOH1046 |
| A | HOH1159 |
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 | 12 |
| Details | BINDING: |
| Chain | Residue | Details |
| B | ASP260 | |
| D | PHE327 | |
| D | ARG387 | |
| D | PRO389 | |
| B | GLN299 | |
| B | ALA326 | |
| B | PHE327 | |
| B | ARG387 | |
| B | PRO389 | |
| D | ASP260 | |
| D | GLN299 | |
| D | ALA326 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:2117606 |
| Chain | Residue | Details |
| B | PRO163 | |
| D | PRO163 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| B | ASN190 | |
| D | ASN190 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 570 |
| Chain | Residue | Details |
| B | LEU325 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| B | PHE327 | metal ligand |
| B | ARG387 | electrostatic stabiliser, hydrogen bond donor |
| B | LEU390 | electrostatic stabiliser, hydrogen bond acceptor |
| B | TYR391 | activator, electrostatic stabiliser, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 570 |
| Chain | Residue | Details |
| D | LEU325 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| D | PHE327 | metal ligand |
| D | ARG387 | electrostatic stabiliser, hydrogen bond donor |
| D | LEU390 | electrostatic stabiliser, hydrogen bond acceptor |
| D | TYR391 | activator, electrostatic stabiliser, proton acceptor, proton donor |
