7D66
Crystal structure of retroviral protease-like domain of Ddi1 from Toxoplasma gondii
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004190 | molecular_function | aspartic-type endopeptidase activity |
A | 0006508 | biological_process | proteolysis |
B | 0004190 | molecular_function | aspartic-type endopeptidase activity |
B | 0006508 | biological_process | proteolysis |
C | 0004190 | molecular_function | aspartic-type endopeptidase activity |
C | 0006508 | biological_process | proteolysis |
D | 0004190 | molecular_function | aspartic-type endopeptidase activity |
D | 0006508 | biological_process | proteolysis |
E | 0004190 | molecular_function | aspartic-type endopeptidase activity |
E | 0006508 | biological_process | proteolysis |
F | 0004190 | molecular_function | aspartic-type endopeptidase activity |
F | 0006508 | biological_process | proteolysis |
G | 0004190 | molecular_function | aspartic-type endopeptidase activity |
G | 0006508 | biological_process | proteolysis |
H | 0004190 | molecular_function | aspartic-type endopeptidase activity |
H | 0006508 | biological_process | proteolysis |
I | 0004190 | molecular_function | aspartic-type endopeptidase activity |
I | 0006508 | biological_process | proteolysis |
J | 0004190 | molecular_function | aspartic-type endopeptidase activity |
J | 0006508 | biological_process | proteolysis |
K | 0004190 | molecular_function | aspartic-type endopeptidase activity |
K | 0006508 | biological_process | proteolysis |
L | 0004190 | molecular_function | aspartic-type endopeptidase activity |
L | 0006508 | biological_process | proteolysis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue GOL B 451 |
Chain | Residue |
B | THR420 |
B | GOL452 |
B | HOH516 |
B | HOH517 |
site_id | AC2 |
Number of Residues | 1 |
Details | binding site for residue GOL B 452 |
Chain | Residue |
B | GOL451 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue GOL B 453 |
Chain | Residue |
B | TYR325 |
F | GLN377 |
I | GLN377 |
I | HOH517 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue GOL B 454 |
Chain | Residue |
B | TYR325 |
B | MET337 |
B | VAL354 |
F | SER324 |
F | ALA326 |
F | GLN377 |
site_id | AC5 |
Number of Residues | 1 |
Details | binding site for residue GOL A 451 |
Chain | Residue |
A | GLN366 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue GOL A 452 |
Chain | Residue |
A | THR339 |
A | ARG340 |
A | TYR341 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue GOL A 453 |
Chain | Residue |
A | LYS356 |
A | HIS358 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue GOL F 451 |
Chain | Residue |
F | VAL348 |
F | HOH504 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue GOL F 452 |
Chain | Residue |
F | ASP338 |
F | ARG340 |
F | LYS356 |
F | HIS358 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue GOL F 453 |
Chain | Residue |
F | ARG340 |
F | ARG342 |
F | GLU352 |
F | ILE353 |
site_id | AD2 |
Number of Residues | 3 |
Details | binding site for residue GOL F 454 |
Chain | Residue |
F | LYS350 |
F | HOH519 |
F | HOH521 |
site_id | AD3 |
Number of Residues | 3 |
Details | binding site for residue GOL E 451 |
Chain | Residue |
E | SER320 |
E | THR374 |
E | HOH511 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue GOL H 451 |
Chain | Residue |
H | ARG340 |
H | LYS356 |
H | HIS358 |
H | HOH505 |
H | HOH506 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue GOL J 451 |
Chain | Residue |
J | PRO370 |
J | SER371 |
J | ARG392 |
site_id | AD6 |
Number of Residues | 2 |
Details | binding site for residue GOL I 451 |
Chain | Residue |
I | GLN319 |
I | HOH505 |
site_id | AD7 |
Number of Residues | 1 |
Details | binding site for residue GOL L 451 |
Chain | Residue |
L | LYS356 |