1UQT
Trehalose-6-phosphate from E. coli bound with UDP-2-fluoro 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 | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0016758 | molecular_function | hexosyltransferase activity |
| A | 0070415 | biological_process | trehalose metabolism in response to cold stress |
| 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 | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0016758 | molecular_function | hexosyltransferase activity |
| B | 0070415 | biological_process | trehalose metabolism in response to cold stress |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE U2F A 900 |
| 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 | HOH2008 |
| A | HOH2071 |
| A | HOH2072 |
| A | GLN185 |
| A | ILE225 |
| A | VAL260 |
| A | ARG262 |
| A | LYS267 |
| A | PRO297 |
| A | HIS338 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE U2F B 901 |
| Chain | Residue |
| B | TRP85 |
| B | HIS154 |
| B | GLN185 |
| B | ILE225 |
| B | VAL260 |
| B | ARG262 |
| B | LYS267 |
| B | PRO297 |
| B | HIS338 |
| B | PHE339 |
| B | ARG341 |
| B | LEU344 |
| B | ASP361 |
| B | GLY362 |
| B | MET363 |
| B | ASN364 |
| B | LEU365 |
| B | VAL366 |
| B | GLU369 |
| B | HOH2001 |
| B | HOH2031 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12498887, ECO:0000269|PubMed:20077550, ECO:0007744|PDB:1GZ5, ECO:0007744|PDB:2WTX |
| Chain | Residue | Details |
| A | ILE10 | |
| A | ASN77 | |
| A | TYR131 | |
| A | GLY301 | |
| B | ILE10 | |
| B | ASN77 | |
| B | TYR131 | |
| B | GLY301 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:12498887, ECO:0000305|PubMed:14570926, ECO:0000305|PubMed:20077550, ECO:0007744|PDB:1GZ5, ECO:0007744|PDB:2WTX |
| Chain | Residue | Details |
| A | GLY22 | |
| B | GLY22 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:12498887, ECO:0000305|PubMed:14570926, ECO:0000305|PubMed:20077550, ECO:0007744|PDB:1GZ5, ECO:0007744|PDB:1UQT, ECO:0007744|PDB:1UQU, ECO:0007744|PDB:2WTX |
| Chain | Residue | Details |
| A | LEU263 | |
| A | GLY268 | |
| A | ASP340 | |
| A | VAL366 | |
| B | LEU263 | |
| B | GLY268 | |
| B | ASP340 | |
| B | VAL366 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | SITE: Involved in alpha anomer selectivity => ECO:0000305|PubMed:12498887 |
| Chain | Residue | Details |
| A | PRO86 | |
| A | PRO156 | |
| B | PRO86 | |
| B | PRO156 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 12498887 |
| Chain | Residue | Details |
| A | ASP361 | |
| A | HIS154 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 12498887 |
| Chain | Residue | Details |
| B | ASP361 | |
| B | HIS154 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 622 |
| Chain | Residue | Details |
| A | ILE155 | electrostatic stabiliser |
| A | GLY362 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 622 |
| Chain | Residue | Details |
| B | ILE155 | electrostatic stabiliser |
| B | GLY362 | electrostatic stabiliser |
