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 | 8 |
Details | binding site for residue WJG A 501 |
Chain | Residue |
A | GLY119 |
A | GLU121 |
A | TYR150 |
A | ASP192 |
A | GLN195 |
A | LEU196 |
A | LEU390 |
A | HOH619 |
site_id | AC2 |
Number of Residues | 1 |
Details | binding site for residue DMS A 502 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue DMS A 503 |
Chain | Residue |
A | SER294 |
A | TYR296 |
A | LEU321 |
A | HOH637 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue EDO A 504 |
Chain | Residue |
A | SER197 |
A | GLU198 |
A | ASP199 |
A | ARG202 |
A | HOH608 |
A | HOH698 |
A | HOH712 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue EDO A 505 |
Chain | Residue |
A | LYS162 |
A | ASN185 |
A | ARG217 |
A | HOH626 |
A | HOH636 |
A | HOH676 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue EDO A 506 |
Chain | Residue |
A | ARG217 |
A | VAL298 |
A | ASP299 |
A | LEU300 |
A | HOH682 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue EDO A 507 |
Chain | Residue |
A | ARG210 |
A | GLU252 |
A | PHE253 |
A | ARG254 |
A | HOH601 |
A | HOH612 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue EDO A 508 |
Chain | Residue |
A | GLU159 |
A | GLY238 |
A | ASP239 |
A | GLY276 |
A | MET277 |
A | ARG371 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue EDO A 509 |
Chain | Residue |
A | TYR189 |
A | ASP212 |
A | ARG217 |
A | VAL298 |
A | HOH615 |
A | HOH682 |
A | HOH720 |
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 | |