Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003779 | molecular_function | actin binding |
A | 0006470 | biological_process | protein dephosphorylation |
A | 0016311 | biological_process | dephosphorylation |
A | 0016791 | molecular_function | phosphatase activity |
A | 0030837 | biological_process | negative regulation of actin filament polymerization |
B | 0003779 | molecular_function | actin binding |
B | 0006470 | biological_process | protein dephosphorylation |
B | 0016311 | biological_process | dephosphorylation |
B | 0016791 | molecular_function | phosphatase activity |
B | 0030837 | biological_process | negative regulation of actin filament polymerization |
C | 0003779 | molecular_function | actin binding |
C | 0006470 | biological_process | protein dephosphorylation |
C | 0016311 | biological_process | dephosphorylation |
C | 0016791 | molecular_function | phosphatase activity |
C | 0030837 | biological_process | negative regulation of actin filament polymerization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 101 |
Chain | Residue |
A | ASP361 |
A | SER392 |
A | LYS393 |
A | MET394 |
A | GLY395 |
A | VAL396 |
A | SER397 |
A | ARG398 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 B 101 |
Chain | Residue |
B | SER392 |
B | LYS393 |
B | MET394 |
B | GLY395 |
B | VAL396 |
B | SER397 |
B | ARG398 |
B | ASP361 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 C 101 |
Chain | Residue |
C | HOH66 |
C | ASP361 |
C | SER392 |
C | LYS393 |
C | MET394 |
C | GLY395 |
C | VAL396 |
C | SER397 |
C | ARG398 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | SER392 | |
B | SER392 | |
C | SER392 | |