5HVM
Structure of Aspergillus fumigatus trehalose-6-phosphate synthase A in complex with UDP and validoxylamine A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003825 | molecular_function | alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity |
| A | 0004805 | molecular_function | trehalose-phosphatase activity |
| A | 0005946 | cellular_component | alpha,alpha-trehalose-phosphate synthase complex (UDP-forming) |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0005992 | biological_process | trehalose biosynthetic process |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0016758 | molecular_function | hexosyltransferase activity |
| A | 0034605 | biological_process | cellular response to heat |
| A | 0070413 | biological_process | trehalose metabolism in response to stress |
| A | 0102986 | molecular_function | trehalose synthase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003825 | molecular_function | alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity |
| B | 0004805 | molecular_function | trehalose-phosphatase activity |
| B | 0005946 | cellular_component | alpha,alpha-trehalose-phosphate synthase complex (UDP-forming) |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0005992 | biological_process | trehalose biosynthetic process |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0016758 | molecular_function | hexosyltransferase activity |
| B | 0034605 | biological_process | cellular response to heat |
| B | 0070413 | biological_process | trehalose metabolism in response to stress |
| B | 0102986 | molecular_function | trehalose synthase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue UDP A 601 |
| Chain | Residue |
| A | ARG287 |
| A | VDM602 |
| A | HOH701 |
| A | LYS292 |
| A | VAL322 |
| A | SER363 |
| A | VAL364 |
| A | LEU369 |
| A | LEU390 |
| A | VAL391 |
| A | GLU394 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue VDM A 602 |
| Chain | Residue |
| A | TRP106 |
| A | ASP151 |
| A | HIS153 |
| A | HIS179 |
| A | ILE249 |
| A | ARG325 |
| A | ASP386 |
| A | GLY387 |
| A | MET388 |
| A | ASN389 |
| A | LEU390 |
| A | UDP601 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | binding site for residue UDP B 601 |
| Chain | Residue |
| B | VAL285 |
| B | ARG287 |
| B | LYS292 |
| B | VAL322 |
| B | SER363 |
| B | VAL364 |
| B | LEU369 |
| B | ASN389 |
| B | LEU390 |
| B | VAL391 |
| B | GLU394 |
| B | VDM602 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue VDM B 602 |
| Chain | Residue |
| B | TRP106 |
| B | ASP151 |
| B | HIS179 |
| B | ARG287 |
| B | ARG325 |
| B | ASP386 |
| B | GLY387 |
| B | MET388 |
| B | ASN389 |
| B | UDP601 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q92410 |
| Chain | Residue | Details |
| A | TYR97 | |
| B | LYS292 | |
| B | ARG325 | |
| B | ASP386 | |
| A | ASP151 | |
| A | ARG287 | |
| A | LYS292 | |
| A | ARG325 | |
| A | ASP386 | |
| B | TYR97 | |
| B | ASP151 | |
| B | ARG287 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:28743811, ECO:0007744|PDB:5HVM |
| Chain | Residue | Details |
| A | VAL364 | |
| A | LEU390 | |
| B | VAL364 | |
| B | LEU390 |
