1YRO
Crystal structure of beta14,-galactosyltransferase mutant ARG228Lys in complex with alpha-lactalbumin in the presence of UDP-galactose and Mn
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 | 0005615 | cellular_component | extracellular space |
| 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 |
| A | 0140767 | molecular_function | enzyme-substrate adaptor activity |
| 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 | 0005615 | cellular_component | extracellular space |
| 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 |
| C | 0140767 | molecular_function | enzyme-substrate adaptor activity |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0016757 | molecular_function | glycosyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE GDU B 403 |
| Chain | Residue |
| A | HOH1139 |
| B | ASP254 |
| B | LYS279 |
| B | GLY292 |
| B | TRP314 |
| B | GLY315 |
| B | GLU317 |
| B | ASP318 |
| B | MET344 |
| B | HIS347 |
| B | ARG349 |
| B | PRO187 |
| B | ASP350 |
| B | MN404 |
| B | HOH909 |
| B | HOH915 |
| B | HOH958 |
| B | HOH964 |
| B | HOH1036 |
| B | HOH1122 |
| B | HOH1166 |
| B | PHE188 |
| B | ARG189 |
| B | ARG191 |
| B | PHE226 |
| B | LYS228 |
| B | ASP252 |
| B | VAL253 |
| site_id | AC2 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE GDU D 528 |
| Chain | Residue |
| D | PRO187 |
| D | PHE188 |
| D | ARG189 |
| D | ARG191 |
| D | PHE226 |
| D | LYS228 |
| D | ASP252 |
| D | VAL253 |
| D | ASP254 |
| D | GLY292 |
| D | TRP314 |
| D | GLY315 |
| D | GLU317 |
| D | ASP318 |
| D | MET344 |
| D | HIS347 |
| D | ASP350 |
| D | ASN353 |
| D | MN529 |
| D | HOH913 |
| D | HOH924 |
| D | HOH946 |
| D | HOH972 |
| D | HOH1032 |
| D | HOH1050 |
| D | HOH1158 |
| D | HOH1354 |
| D | HOH1370 |
| 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 | HOH905 |
| A | HOH942 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA C 124 |
| Chain | Residue |
| C | LYS79 |
| C | ASP82 |
| C | GLU84 |
| C | ASP87 |
| C | ASP88 |
| C | HOH908 |
| C | HOH933 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 404 |
| Chain | Residue |
| B | ASP254 |
| B | MET344 |
| B | HIS347 |
| B | GDU403 |
| B | HOH909 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN D 529 |
| Chain | Residue |
| D | ASP254 |
| D | MET344 |
| D | HIS347 |
| D | GDU528 |
| D | HOH913 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE UDP B 405 |
| Chain | Residue |
| B | LEU155 |
| B | GLU159 |
| B | GLN192 |
| B | TYR388 |
| B | PRO389 |
| B | LEU390 |
| B | TYR391 |
| B | LYS393 |
| B | HOH1199 |
| B | HOH1597 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE UDP D 530 |
| Chain | Residue |
| D | LYS393 |
| D | HOH1163 |
| D | HOH1202 |
| D | HOH1643 |
| D | LEU155 |
| D | LYS156 |
| D | GLU159 |
| D | GLN192 |
| D | GLN386 |
| D | TYR388 |
| D | PRO389 |
| D | LEU390 |
| D | TYR391 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MES A 805 |
| Chain | Residue |
| A | GLU49 |
| A | GLN54 |
| A | LYS99 |
| A | TYR103 |
| A | HOH930 |
| A | HOH1506 |
| site_id | BC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PG4 A 806 |
| Chain | Residue |
| A | PHE31 |
| A | THR33 |
| A | SER34 |
| A | GLY35 |
| A | HOH1139 |
| A | HOH1149 |
| A | HOH1302 |
| A | HOH1320 |
| A | HOH1502 |
| B | PHE280 |
| B | TRP314 |
| site_id | BC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PG4 C 807 |
| Chain | Residue |
| C | PHE31 |
| C | HIS32 |
| C | THR33 |
| C | SER34 |
| C | GLY35 |
| C | ASP37 |
| C | ALA40 |
| C | VAL42 |
| C | HOH927 |
| D | TRP314 |
| D | ARG349 |
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 | 244 |
| Details | Domain: {"description":"C-type lysozyme","evidences":[{"source":"PROSITE-ProRule","id":"PRU00680","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00711","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 32 |
| Details | Binding site: {} |
| Chain | Residue | Details |
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 |
