5L9W
Crystal structure of the Apc core complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006749 | biological_process | glutathione metabolic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016874 | molecular_function | ligase activity |
A | 0017168 | molecular_function | 5-oxoprolinase (ATP-hydrolyzing) activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006749 | biological_process | glutathione metabolic process |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016874 | molecular_function | ligase activity |
B | 0017168 | molecular_function | 5-oxoprolinase (ATP-hydrolyzing) activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0016874 | molecular_function | ligase activity |
b | 0005524 | molecular_function | ATP binding |
b | 0005737 | cellular_component | cytoplasm |
b | 0005829 | cellular_component | cytosol |
b | 0006749 | biological_process | glutathione metabolic process |
b | 0016787 | molecular_function | hydrolase activity |
b | 0016874 | molecular_function | ligase activity |
b | 0017168 | molecular_function | 5-oxoprolinase (ATP-hydrolyzing) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue HG A 701 |
Chain | Residue |
A | ASP65 |
A | HIS123 |
A | ASP126 |
A | HIS148 |
A | HOH803 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue HG A 702 |
Chain | Residue |
A | CYS82 |
A | HOH805 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue K A 703 |
Chain | Residue |
A | ASN501 |
A | THR365 |
A | ASP500 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue EPE A 704 |
Chain | Residue |
A | PRO201 |
A | SER202 |
A | GLN404 |
A | GLY408 |
A | SER409 |
A | SER410 |
B | GLY616 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue HG B 801 |
Chain | Residue |
B | LYS36 |
B | CYS37 |
site_id | AC6 |
Number of Residues | 10 |
Details | binding site for residue EPE B 802 |
Chain | Residue |
B | VAL217 |
B | VAL218 |
B | SER219 |
B | LYS274 |
B | TYR512 |
B | GLU513 |
B | ARG545 |
B | GLU549 |
b | GLN165 |
b | ILE170 |
site_id | AC7 |
Number of Residues | 15 |
Details | binding site for residue ADP b 801 |
Chain | Residue |
b | THR11 |
b | MET12 |
b | ASP14 |
b | ASP274 |
b | VAL275 |
b | GLY276 |
b | GLY277 |
b | THR354 |
b | PHE368 |
b | LEU369 |
b | GLY436 |
b | ASN437 |
b | GLY631 |
b | SER632 |
b | THR635 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue EPE b 802 |
Chain | Residue |
b | HIS33 |
b | ASP34 |
b | TYR35 |
b | THR36 |
b | SER208 |
b | LYS211 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue HG C 201 |
Chain | Residue |
C | CYS22 |
C | CYS25 |
C | CYS75 |
C | CYS78 |
C | ARG80 |