5HUT
Structure of Candida albicans trehalose-6-phosphate synthase in complex 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 | 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 | 0006623 | biological_process | protein targeting to vacuole |
A | 0016757 | molecular_function | glycosyltransferase activity |
A | 0016758 | molecular_function | hexosyltransferase activity |
A | 0030447 | biological_process | filamentous growth |
A | 0034605 | biological_process | cellular response to heat |
A | 0034727 | biological_process | piecemeal microautophagy of the nucleus |
A | 0036168 | biological_process | filamentous growth of a population of unicellular organisms in response to heat |
A | 0036180 | biological_process | filamentous growth of a population of unicellular organisms in response to biotic stimulus |
A | 0070413 | biological_process | trehalose metabolism in response to stress |
A | 0071465 | biological_process | cellular response to desiccation |
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 | 0006623 | biological_process | protein targeting to vacuole |
B | 0016757 | molecular_function | glycosyltransferase activity |
B | 0016758 | molecular_function | hexosyltransferase activity |
B | 0030447 | biological_process | filamentous growth |
B | 0034605 | biological_process | cellular response to heat |
B | 0034727 | biological_process | piecemeal microautophagy of the nucleus |
B | 0036168 | biological_process | filamentous growth of a population of unicellular organisms in response to heat |
B | 0036180 | biological_process | filamentous growth of a population of unicellular organisms in response to biotic stimulus |
B | 0070413 | biological_process | trehalose metabolism in response to stress |
B | 0071465 | biological_process | cellular response to desiccation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 29 |
Details | binding site for residue UPG A 501 |
Chain | Residue |
A | TRP98 |
A | SER356 |
A | ILE357 |
A | LEU362 |
A | ASP379 |
A | GLY380 |
A | MET381 |
A | ASN382 |
A | LEU383 |
A | VAL384 |
A | GLU387 |
A | ASP143 |
A | 1PE507 |
A | HOH608 |
A | HOH612 |
A | HOH623 |
A | HOH642 |
A | HOH669 |
A | HOH672 |
A | HOH700 |
A | HOH731 |
A | HOH760 |
A | HIS171 |
A | HIS202 |
A | VAL278 |
A | ARG280 |
A | LYS285 |
A | VAL315 |
A | ARG318 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 502 |
Chain | Residue |
A | TYR89 |
A | SER317 |
A | ARG318 |
A | HOH677 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue SO4 A 503 |
Chain | Residue |
A | SER176 |
A | SER177 |
A | HIS209 |
A | SER212 |
B | ARG208 |
B | SO4503 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 504 |
Chain | Residue |
A | ARG186 |
A | LYS187 |
A | HOH615 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue SO4 A 505 |
Chain | Residue |
A | ARG395 |
A | HOH699 |
site_id | AC6 |
Number of Residues | 8 |
Details | binding site for residue 1PE A 506 |
Chain | Residue |
A | SER326 |
A | SER329 |
A | THR330 |
A | GLU333 |
A | HOH726 |
B | SER326 |
B | SER329 |
B | GLU333 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue 1PE A 507 |
Chain | Residue |
A | SER31 |
A | THR36 |
A | ILE357 |
A | PRO358 |
A | PHE359 |
A | UPG501 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue NA A 508 |
Chain | Residue |
A | PHE269 |
A | VAL272 |
A | HOH699 |
A | HOH732 |
A | HOH793 |
site_id | AC9 |
Number of Residues | 23 |
Details | binding site for residue UPG B 501 |
Chain | Residue |
B | HIS171 |
B | HIS202 |
B | ARG280 |
B | LYS285 |
B | VAL315 |
B | SER356 |
B | ILE357 |
B | LEU362 |
B | ASP379 |
B | GLY380 |
B | MET381 |
B | ASN382 |
B | LEU383 |
B | VAL384 |
B | GLU387 |
B | 1PE507 |
B | HOH614 |
B | HOH639 |
B | HOH645 |
B | HOH712 |
B | HOH719 |
B | HOH732 |
B | HOH756 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 502 |
Chain | Residue |
B | TYR89 |
B | SER317 |
B | ARG318 |
B | HOH639 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue SO4 B 503 |
Chain | Residue |
A | ARG208 |
A | SO4503 |
B | SER176 |
B | SER177 |
B | HIS209 |
B | SER212 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 505 |
Chain | Residue |
B | HOH730 |
B | LYS266 |
B | ARG395 |
B | HOH656 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue SO4 B 504 |
Chain | Residue |
B | ARG186 |
B | HOH631 |
B | HOH665 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue 1PE B 506 |
Chain | Residue |
B | THR63 |
B | LYS270 |
B | ASP271 |
B | LYS273 |
B | GLU303 |
site_id | AD6 |
Number of Residues | 3 |
Details | binding site for residue 1PE B 507 |
Chain | Residue |
B | ASN248 |
B | PHE359 |
B | UPG501 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue NA B 508 |
Chain | Residue |
B | PHE269 |
B | VAL272 |
B | HOH656 |
B | HOH686 |
B | HOH730 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:28743811, ECO:0007744|PDB:5HUU |
Chain | Residue | Details |
A | TYR89 | |
A | ASP143 | |
A | ARG318 | |
A | LEU383 | |
B | TYR89 | |
B | ASP143 | |
B | ARG318 | |
B | LEU383 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:28743811, ECO:0007744|PDB:5HUT |
Chain | Residue | Details |
A | ARG280 | |
A | LYS285 | |
A | ILE357 | |
A | ASP379 | |
B | ARG280 | |
B | LYS285 | |
B | ILE357 | |
B | ASP379 |