5HVO
Structure of Aspergillus fumigatus trehalose-6-phosphate synthase B 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 | 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 | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0034605 | biological_process | cellular response to heat |
| 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 | 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 | 0016740 | molecular_function | transferase activity |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0034605 | biological_process | cellular response to heat |
| B | 0102986 | molecular_function | trehalose synthase activity |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0003825 | molecular_function | alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity |
| C | 0005946 | cellular_component | alpha,alpha-trehalose-phosphate synthase complex (UDP-forming) |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0005992 | biological_process | trehalose biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016757 | molecular_function | glycosyltransferase activity |
| C | 0034605 | biological_process | cellular response to heat |
| C | 0102986 | molecular_function | trehalose synthase activity |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0003825 | molecular_function | alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity |
| D | 0005946 | cellular_component | alpha,alpha-trehalose-phosphate synthase complex (UDP-forming) |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0005992 | biological_process | trehalose biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016757 | molecular_function | glycosyltransferase activity |
| D | 0034605 | biological_process | cellular response to heat |
| D | 0102986 | molecular_function | trehalose synthase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue UDP A 501 |
| Chain | Residue |
| A | VAL285 |
| A | VAL391 |
| A | GLU394 |
| A | VDM502 |
| A | HOH623 |
| A | HOH631 |
| A | ARG287 |
| A | LYS292 |
| A | VAL322 |
| A | SER363 |
| A | VAL364 |
| A | LEU369 |
| A | ASN389 |
| A | LEU390 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue VDM A 502 |
| Chain | Residue |
| A | TRP105 |
| A | ASP150 |
| A | HIS152 |
| A | HIS179 |
| A | ASP386 |
| A | GLY387 |
| A | MET388 |
| A | ASN389 |
| A | UDP501 |
| A | HOH617 |
| A | HOH622 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue UDP B 501 |
| Chain | Residue |
| B | VAL285 |
| B | ARG287 |
| B | LYS292 |
| B | VAL322 |
| B | SER363 |
| B | VAL364 |
| B | LEU369 |
| B | LEU390 |
| B | VAL391 |
| B | GLU394 |
| B | VDM502 |
| B | HOH614 |
| B | HOH633 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for residue VDM B 502 |
| Chain | Residue |
| B | ASP150 |
| B | HIS152 |
| B | HIS179 |
| B | ARG287 |
| B | ARG325 |
| B | ASP386 |
| B | GLY387 |
| B | MET388 |
| B | ASN389 |
| B | LEU390 |
| B | UDP501 |
| B | HOH613 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | binding site for residue UDP C 501 |
| Chain | Residue |
| C | VAL285 |
| C | ARG287 |
| C | LYS292 |
| C | VAL322 |
| C | SER363 |
| C | VAL364 |
| C | LEU369 |
| C | LEU390 |
| C | VAL391 |
| C | GLU394 |
| C | VDM502 |
| C | HOH609 |
| C | HOH614 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | binding site for residue VDM C 502 |
| Chain | Residue |
| C | ASP150 |
| C | HIS152 |
| C | HIS179 |
| C | ILE249 |
| C | ARG325 |
| C | ASP386 |
| C | GLY387 |
| C | MET388 |
| C | ASN389 |
| C | LEU390 |
| C | UDP501 |
| C | HOH615 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | binding site for residue UDP D 501 |
| Chain | Residue |
| D | ARG287 |
| D | LYS292 |
| D | VAL322 |
| D | SER363 |
| D | VAL364 |
| D | LEU369 |
| D | LEU390 |
| D | VAL391 |
| D | GLU394 |
| D | VDM502 |
| D | HOH622 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | binding site for residue VDM D 502 |
| Chain | Residue |
| D | ASP150 |
| D | HIS152 |
| D | HIS179 |
| D | ARG287 |
| D | ARG325 |
| D | ASP386 |
| D | GLY387 |
| D | MET388 |
| D | ASN389 |
| D | LEU390 |
| D | UDP501 |
| D | HOH619 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 52 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q92410","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28743811","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5HVO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
