6M7Z
A divergent kinase lacking the glycine-rich loop regulates membrane ultrastructure of the Toxoplasma parasitophorous vacuole
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005615 | cellular_component | extracellular space |
A | 0006468 | biological_process | protein phosphorylation |
A | 0097570 | cellular_component | cyst wall |
B | 0004672 | molecular_function | protein kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005576 | cellular_component | extracellular region |
B | 0005615 | cellular_component | extracellular space |
B | 0006468 | biological_process | protein phosphorylation |
B | 0097570 | cellular_component | cyst wall |
C | 0004672 | molecular_function | protein kinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005576 | cellular_component | extracellular region |
C | 0005615 | cellular_component | extracellular space |
C | 0006468 | biological_process | protein phosphorylation |
C | 0097570 | cellular_component | cyst wall |
D | 0004672 | molecular_function | protein kinase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0005576 | cellular_component | extracellular region |
D | 0005615 | cellular_component | extracellular space |
D | 0006468 | biological_process | protein phosphorylation |
D | 0097570 | cellular_component | cyst wall |
E | 0004672 | molecular_function | protein kinase activity |
E | 0005524 | molecular_function | ATP binding |
E | 0005576 | cellular_component | extracellular region |
E | 0005615 | cellular_component | extracellular space |
E | 0006468 | biological_process | protein phosphorylation |
E | 0097570 | cellular_component | cyst wall |
F | 0004672 | molecular_function | protein kinase activity |
F | 0005524 | molecular_function | ATP binding |
F | 0005576 | cellular_component | extracellular region |
F | 0005615 | cellular_component | extracellular space |
F | 0006468 | biological_process | protein phosphorylation |
F | 0097570 | cellular_component | cyst wall |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue EDO A 401 |
Chain | Residue |
A | GLY192 |
A | GLU196 |
A | ASN301 |
A | LEU305 |
A | HOH529 |
C | ARG113 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue EDO A 402 |
Chain | Residue |
A | THR180 |
A | TYR181 |
A | LYS137 |
A | ARG139 |
A | GLU152 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue EDO B 401 |
Chain | Residue |
B | LEU160 |
B | PRO161 |
B | ARG163 |
B | SER164 |
B | LEU167 |
B | PRO169 |
B | HOH518 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue EDO B 402 |
Chain | Residue |
B | GLU132 |
B | PRO237 |
B | ASP238 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue EDO B 403 |
Chain | Residue |
B | TYR156 |
B | GLU173 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue EDO B 404 |
Chain | Residue |
B | LYS137 |
B | VAL138 |
B | ARG139 |
B | SER149 |
B | GLU152 |
B | THR180 |
B | ILE182 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue EDO C 401 |
Chain | Residue |
C | SER290 |
C | PRO339 |
C | ARG342 |
C | EDO403 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue EDO C 402 |
Chain | Residue |
B | ARG113 |
C | GLY192 |
C | GLU196 |
C | ASN301 |
C | HOH521 |
site_id | AC9 |
Number of Residues | 1 |
Details | binding site for residue EDO C 403 |
Chain | Residue |
C | EDO401 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue EDO C 404 |
Chain | Residue |
C | LYS137 |
C | ARG139 |
C | GLU152 |
C | THR180 |
C | HOH558 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue EDO C 405 |
Chain | Residue |
C | GLU132 |
C | PRO185 |
C | PRO237 |
C | ASP238 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue EDO C 406 |
Chain | Residue |
C | ARG157 |
C | GLU158 |
C | LEU160 |
D | HOH408 |
site_id | AD4 |
Number of Residues | 1 |
Details | binding site for residue CL C 407 |
Chain | Residue |
C | ASP86 |
site_id | AD5 |
Number of Residues | 6 |
Details | binding site for residue EDO E 401 |
Chain | Residue |
D | ARG113 |
E | GLY192 |
E | GLU196 |
E | ASN301 |
E | LEU305 |
E | HOH517 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue EDO E 402 |
Chain | Residue |
E | LYS137 |
E | ARG139 |
E | SER149 |
E | GLU152 |
E | THR180 |
site_id | AD7 |
Number of Residues | 3 |
Details | binding site for residue CL E 403 |
Chain | Residue |
E | GLY176 |
E | ALA177 |
E | TYR181 |
site_id | AD8 |
Number of Residues | 3 |
Details | binding site for residue EDO F 401 |
Chain | Residue |
F | GLU132 |
F | PRO237 |
F | ASP238 |
site_id | AD9 |
Number of Residues | 6 |
Details | binding site for residue EDO F 402 |
Chain | Residue |
F | LYS137 |
F | ARG139 |
F | SER149 |
F | GLU152 |
F | THR180 |
F | ILE182 |