5CPQ
Disproportionating enzyme 1 from Arabidopsis - apo form
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000025 | biological_process | maltose catabolic process |
A | 0000272 | biological_process | polysaccharide catabolic process |
A | 0004134 | molecular_function | 4-alpha-glucanotransferase activity |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0005983 | biological_process | starch catabolic process |
A | 0006006 | biological_process | glucose metabolic process |
A | 0009501 | cellular_component | amyloplast |
A | 0009507 | cellular_component | chloroplast |
A | 0009536 | cellular_component | plastid |
A | 0016740 | molecular_function | transferase activity |
A | 0016757 | molecular_function | glycosyltransferase activity |
B | 0000025 | biological_process | maltose catabolic process |
B | 0000272 | biological_process | polysaccharide catabolic process |
B | 0004134 | molecular_function | 4-alpha-glucanotransferase activity |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0005983 | biological_process | starch catabolic process |
B | 0006006 | biological_process | glucose metabolic process |
B | 0009501 | cellular_component | amyloplast |
B | 0009507 | cellular_component | chloroplast |
B | 0009536 | cellular_component | plastid |
B | 0016740 | molecular_function | transferase activity |
B | 0016757 | molecular_function | glycosyltransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | binding site for residue EDO A 601 |
Chain | Residue |
A | THR188 |
A | PHE261 |
A | LYS268 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue EDO A 602 |
Chain | Residue |
A | TYR367 |
A | HOH703 |
A | HOH738 |
A | ALA141 |
A | ASN142 |
A | MET294 |
A | ARG359 |
A | ARG362 |
A | ALA363 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue EDO A 603 |
Chain | Residue |
A | PRO295 |
A | ILE296 |
A | TYR297 |
A | ASP373 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue EDO A 604 |
Chain | Residue |
A | ALA363 |
A | GLN364 |
A | TYR367 |
A | ASP368 |
A | ILE415 |
A | LYS416 |
site_id | AC5 |
Number of Residues | 8 |
Details | binding site for residue EDO A 605 |
Chain | Residue |
A | THR471 |
A | HIS472 |
A | ASN474 |
A | PRO523 |
A | GLN525 |
A | MET536 |
A | EDO606 |
A | HOH728 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue EDO A 606 |
Chain | Residue |
A | LEU87 |
A | HIS472 |
A | GLN525 |
A | MET536 |
A | EDO605 |
A | HOH791 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue EDO B 800 |
Chain | Residue |
B | THR188 |
B | PHE261 |
B | LEU264 |
B | PHE265 |
B | LYS268 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue EDO B 801 |
Chain | Residue |
B | PRO295 |
B | ILE296 |
B | TYR297 |
B | ASP373 |
site_id | AC9 |
Number of Residues | 9 |
Details | binding site for residue EDO B 802 |
Chain | Residue |
B | ALA141 |
B | ASN142 |
B | MET294 |
B | ARG359 |
B | ARG362 |
B | ALA363 |
B | TYR367 |
B | HOH913 |
B | HOH926 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue EDO B 803 |
Chain | Residue |
B | ALA363 |
B | TYR367 |
B | ASP368 |
B | CYS370 |
B | ILE415 |
B | LYS416 |
site_id | AD2 |
Number of Residues | 2 |
Details | binding site for residue EDO B 804 |
Chain | Residue |
B | ASP220 |
B | ARG246 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue EDO B 805 |
Chain | Residue |
B | LEU87 |
B | GLN525 |
B | MET536 |
B | TRP548 |
B | EDO806 |
B | HOH1011 |
site_id | AD4 |
Number of Residues | 9 |
Details | binding site for residue EDO B 806 |
Chain | Residue |
B | THR471 |
B | HIS472 |
B | ASN474 |
B | THR476 |
B | PRO523 |
B | GLN525 |
B | MET536 |
B | EDO805 |
B | HOH1010 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue EDO B 807 |
Chain | Residue |
B | ARG535 |
B | THR538 |
B | GLY544 |
B | ASN545 |