2WTX
Insight into the mechanism of enzymatic glycosyltransfer with retention through the synthesis and analysis of bisubstrate glycomimetics of trehalose-6-phosphate synthase
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 |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0003825 | molecular_function | alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity |
| C | 0005992 | biological_process | trehalose biosynthetic process |
| C | 0006950 | biological_process | response to stress |
| C | 0006970 | biological_process | response to osmotic stress |
| C | 0006974 | biological_process | DNA damage response |
| C | 0016757 | molecular_function | glycosyltransferase activity |
| C | 0016758 | molecular_function | hexosyltransferase activity |
| C | 0070415 | biological_process | trehalose metabolism in response to cold stress |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0003825 | molecular_function | alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity |
| D | 0005992 | biological_process | trehalose biosynthetic process |
| D | 0006950 | biological_process | response to stress |
| D | 0006970 | biological_process | response to osmotic stress |
| D | 0006974 | biological_process | DNA damage response |
| D | 0016757 | molecular_function | glycosyltransferase activity |
| D | 0016758 | molecular_function | hexosyltransferase activity |
| D | 0070415 | biological_process | trehalose metabolism in response to cold stress |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1457 |
| Chain | Residue |
| A | THR298 |
| A | SER299 |
| A | ARG300 |
| A | GLY301 |
| A | HOH2196 |
| A | HOH2201 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 1459 |
| Chain | Residue |
| B | PRO402 |
| B | TYR403 |
| B | ARG405 |
| A | PHE97 |
| A | HOH2041 |
| B | GLU271 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1458 |
| Chain | Residue |
| A | HIS89 |
| A | ARG91 |
| A | LEU359 |
| A | TYR403 |
| A | HOH2036 |
| A | HOH2100 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 1459 |
| Chain | Residue |
| A | ASP180 |
| A | ALA217 |
| A | PHE218 |
| A | ARG219 |
| A | ILE453 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 1460 |
| Chain | Residue |
| B | ASN77 |
| B | ARG300 |
| B | GLY301 |
| B | ASP302 |
| B | HOH2147 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE UDP A 1460 |
| Chain | Residue |
| A | ALA20 |
| A | GLY21 |
| A | GLY22 |
| A | VAL25 |
| A | VAL260 |
| A | ARG262 |
| A | LYS267 |
| A | HIS338 |
| A | PHE339 |
| A | ARG341 |
| A | LEU344 |
| A | ASN364 |
| A | LEU365 |
| A | VAL366 |
| A | GLU369 |
| A | VDO1461 |
| A | HOH2197 |
| A | HOH2198 |
| A | HOH2199 |
| site_id | AC7 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE VDO A 1461 |
| Chain | Residue |
| A | ARG9 |
| A | GLY22 |
| A | LEU23 |
| A | TYR76 |
| A | TRP85 |
| A | ASP130 |
| A | HIS132 |
| A | HIS154 |
| A | ILE155 |
| A | GLN185 |
| A | ILE225 |
| A | ARG262 |
| A | ARG300 |
| A | ASP361 |
| A | GLY362 |
| A | MET363 |
| A | ASN364 |
| A | LEU365 |
| A | UDP1460 |
| A | HOH2005 |
| A | HOH2013 |
| A | HOH2015 |
| A | HOH2033 |
| A | HOH2200 |
| A | HOH2201 |
| A | HOH2202 |
| site_id | AC8 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE UDP B 1461 |
| Chain | Residue |
| B | ALA20 |
| B | GLY21 |
| B | GLY22 |
| B | VAL260 |
| B | ARG262 |
| B | LYS267 |
| B | HIS338 |
| B | PHE339 |
| B | ARG341 |
| B | LEU344 |
| B | ASN364 |
| B | LEU365 |
| B | VAL366 |
| B | GLU369 |
| B | VDO1462 |
| B | HOH2148 |
| B | HOH2149 |
| site_id | AC9 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE VDO B 1462 |
| Chain | Residue |
| B | HIS132 |
| B | HIS154 |
| B | ILE155 |
| B | ILE225 |
| B | ARG262 |
| B | ARG300 |
| B | ASP361 |
| B | GLY362 |
| B | MET363 |
| B | ASN364 |
| B | LEU365 |
| B | UDP1461 |
| B | HOH2010 |
| B | HOH2030 |
| B | HOH2150 |
| B | HOH2151 |
| B | HOH2152 |
| B | ARG9 |
| B | ALA20 |
| B | GLY21 |
| B | GLY22 |
| B | LEU23 |
| B | TYR76 |
| B | TRP85 |
| B | ASP130 |
| B | TYR131 |
| site_id | BC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE UDP C 1457 |
| Chain | Residue |
| C | VAL260 |
| C | ARG262 |
| C | LYS267 |
| C | HIS338 |
| C | PHE339 |
| C | ARG341 |
| C | LEU344 |
| C | ASN364 |
| C | LEU365 |
| C | VAL366 |
| C | GLU369 |
| C | VDO1458 |
| C | HOH2073 |
| C | HOH2074 |
| site_id | BC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE VDO C 1458 |
| Chain | Residue |
| C | ASP130 |
| C | HIS154 |
| C | GLN185 |
| C | ILE225 |
| C | ARG262 |
| C | ARG300 |
| C | ASP361 |
| C | GLY362 |
| C | MET363 |
| C | ASN364 |
| C | LEU365 |
| C | UDP1457 |
| C | HOH2057 |
| C | HOH2075 |
| site_id | BC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE UDP D 1458 |
| Chain | Residue |
| D | VAL260 |
| D | ARG262 |
| D | LYS267 |
| D | HIS338 |
| D | PHE339 |
| D | ARG341 |
| D | LEU344 |
| D | ASN364 |
| D | LEU365 |
| D | VAL366 |
| D | GLU369 |
| D | VDO1459 |
| D | HOH2145 |
| D | HOH2147 |
| D | HOH2148 |
| D | HOH2149 |
| D | HOH2151 |
| D | HOH2152 |
| site_id | BC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE VDO D 1459 |
| Chain | Residue |
| D | TRP85 |
| D | ASP130 |
| D | HIS132 |
| D | HIS154 |
| D | ILE155 |
| D | ILE225 |
| D | ARG262 |
| D | ARG300 |
| D | ASP361 |
| D | GLY362 |
| D | MET363 |
| D | ASN364 |
| D | LEU365 |
| D | UDP1458 |
| D | HOH2153 |
| D | HOH2154 |
| D | HOH2155 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12498887, ECO:0000269|PubMed:20077550, ECO:0007744|PDB:1GZ5, ECO:0007744|PDB:2WTX |
| Chain | Residue | Details |
| A | ARG9 | |
| C | TYR76 | |
| C | ASP130 | |
| C | ARG300 | |
| D | ARG9 | |
| D | TYR76 | |
| D | ASP130 | |
| D | ARG300 | |
| A | TYR76 | |
| A | ASP130 | |
| A | ARG300 | |
| B | ARG9 | |
| B | TYR76 | |
| B | ASP130 | |
| B | ARG300 | |
| C | ARG9 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| 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 | GLY21 | |
| B | GLY21 | |
| C | GLY21 | |
| D | GLY21 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| 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 | ARG262 | |
| C | LYS267 | |
| C | PHE339 | |
| C | LEU365 | |
| D | ARG262 | |
| D | LYS267 | |
| D | PHE339 | |
| D | LEU365 | |
| A | LYS267 | |
| A | PHE339 | |
| A | LEU365 | |
| B | ARG262 | |
| B | LYS267 | |
| B | PHE339 | |
| B | LEU365 | |
| C | ARG262 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | SITE: Involved in alpha anomer selectivity => ECO:0000305|PubMed:12498887 |
| Chain | Residue | Details |
| A | TRP85 | |
| A | ILE155 | |
| B | TRP85 | |
| B | ILE155 | |
| C | TRP85 | |
| C | ILE155 | |
| D | TRP85 | |
| D | ILE155 |
Catalytic Information from CSA
| 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 |
| site_id | MCSA3 |
| Number of Residues | 2 |
| Details | M-CSA 622 |
| Chain | Residue | Details |
| C | HIS154 | electrostatic stabiliser |
| C | ASP361 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 2 |
| Details | M-CSA 622 |
| Chain | Residue | Details |
| D | HIS154 | electrostatic stabiliser |
| D | ASP361 | electrostatic stabiliser |
