1UQU
Trehalose-6-phosphate from E. coli bound with UDP-glucose.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0003825 | molecular_function | alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity |
A | 0005992 | biological_process | trehalose biosynthetic process |
A | 0006950 | biological_process | response to stress |
A | 0006970 | biological_process | response to osmotic stress |
A | 0006974 | biological_process | DNA damage response |
A | 0016740 | molecular_function | transferase activity |
A | 0016757 | molecular_function | glycosyltransferase activity |
A | 0016758 | molecular_function | hexosyltransferase activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0003825 | molecular_function | alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity |
B | 0005992 | biological_process | trehalose biosynthetic process |
B | 0006950 | biological_process | response to stress |
B | 0006970 | biological_process | response to osmotic stress |
B | 0006974 | biological_process | DNA damage response |
B | 0016740 | molecular_function | transferase activity |
B | 0016757 | molecular_function | glycosyltransferase activity |
B | 0016758 | molecular_function | hexosyltransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE UPG A1457 |
Chain | Residue |
A | TRP85 |
A | PHE339 |
A | ARG341 |
A | LEU344 |
A | ASP361 |
A | GLY362 |
A | MET363 |
A | ASN364 |
A | LEU365 |
A | VAL366 |
A | GLU369 |
A | HIS154 |
A | HOH2052 |
A | HOH2069 |
A | HOH2070 |
A | HOH2072 |
A | HOH2073 |
A | GLN185 |
A | ILE225 |
A | VAL260 |
A | ARG262 |
A | LYS267 |
A | PRO297 |
A | HIS338 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"12498887","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20077550","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GZ5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WTX","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"12498887","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"14570926","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"20077550","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1GZ5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WTX","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 14 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"12498887","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"14570926","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"20077550","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1GZ5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1UQT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1UQU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WTX","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | Site: {"description":"Involved in alpha anomer selectivity","evidences":[{"source":"PubMed","id":"12498887","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1uqt |
Chain | Residue | Details |
A | ASP361 | |
A | HIS154 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1uqt |
Chain | Residue | Details |
B | ASP361 | |
B | HIS154 |
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 622 |
Chain | Residue | Details |
A | HIS154 | electrostatic stabiliser |
A | ASP361 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 2 |
Details | M-CSA 622 |
Chain | Residue | Details |
B | HIS154 | electrostatic stabiliser |
B | ASP361 | electrostatic stabiliser |