Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005856 | cellular_component | cytoskeleton |
A | 0008092 | molecular_function | cytoskeletal protein binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | binding site for residue NU4 A 401 |
Chain | Residue |
A | ASP149 |
A | TYR150 |
A | PRO191 |
A | PHE386 |
A | PHE387 |
A | LEU389 |
A | LEU390 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue DMS A 402 |
Chain | Residue |
A | LEU117 |
A | GLY119 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue DMS A 403 |
Chain | Residue |
A | SER294 |
A | TYR296 |
A | VAL298 |
A | LEU321 |
A | HOH523 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue EDO A 404 |
Chain | Residue |
A | SER197 |
A | GLU198 |
A | ASP199 |
A | HOH516 |
A | HOH608 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue EDO A 405 |
Chain | Residue |
A | LYS162 |
A | ASN185 |
A | ARG217 |
A | HOH514 |
A | HOH549 |
A | HOH610 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue EDO A 406 |
Chain | Residue |
A | ARG217 |
A | VAL298 |
A | ASP299 |
A | LEU300 |
A | HOH522 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue EDO A 407 |
Chain | Residue |
A | ARG210 |
A | GLU252 |
A | PHE253 |
A | ARG254 |
A | HOH503 |
A | HOH507 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue EDO A 408 |
Chain | Residue |
A | GLY238 |
A | ASP239 |
A | GLY276 |
A | MET277 |
A | ARG371 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue EDO A 409 |
Chain | Residue |
A | TYR189 |
A | ASP212 |
A | ARG217 |
A | VAL298 |
A | HOH504 |
A | HOH522 |
A | HOH622 |
Functional Information from PROSITE/UniProt
site_id | PS00660 |
Number of Residues | 29 |
Details | FERM_1 FERM domain signature 1. WLdpaKeIkkQ..VrsgawhfsFnvk..FYppD |
Chain | Residue | Details |
A | TRP164-ASP192 | |
site_id | PS00661 |
Number of Residues | 30 |
Details | FERM_2 FERM domain signature 2. HkshrgmtpaEAemhFLen.AkkLsmYGvDL |
Chain | Residue | Details |
A | HIS271-LEU300 | |