6I18
CRYSTAL STRUCTURE OF FASCIN IN COMPLEX WITH BDP-13176
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001725 | cellular_component | stress fiber |
A | 0001726 | cellular_component | ruffle |
A | 0002102 | cellular_component | podosome |
A | 0003723 | molecular_function | RNA binding |
A | 0003779 | molecular_function | actin binding |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0005856 | cellular_component | cytoskeleton |
A | 0005902 | cellular_component | microvillus |
A | 0005911 | cellular_component | cell-cell junction |
A | 0005938 | cellular_component | cell cortex |
A | 0007015 | biological_process | actin filament organization |
A | 0007043 | biological_process | cell-cell junction assembly |
A | 0007163 | biological_process | establishment or maintenance of cell polarity |
A | 0008144 | molecular_function | obsolete drug binding |
A | 0010592 | biological_process | positive regulation of lamellipodium assembly |
A | 0015629 | cellular_component | actin cytoskeleton |
A | 0016477 | biological_process | cell migration |
A | 0030027 | cellular_component | lamellipodium |
A | 0030035 | biological_process | microspike assembly |
A | 0030036 | biological_process | actin cytoskeleton organization |
A | 0030046 | biological_process | parallel actin filament bundle assembly |
A | 0030175 | cellular_component | filopodium |
A | 0030426 | cellular_component | growth cone |
A | 0030674 | molecular_function | protein-macromolecule adaptor activity |
A | 0031253 | cellular_component | cell projection membrane |
A | 0032534 | biological_process | regulation of microvillus assembly |
A | 0032956 | biological_process | regulation of actin cytoskeleton organization |
A | 0035089 | biological_process | establishment of apical/basal cell polarity |
A | 0042995 | cellular_component | cell projection |
A | 0044393 | cellular_component | microspike |
A | 0045296 | molecular_function | cadherin binding |
A | 0048870 | biological_process | cell motility |
A | 0051015 | molecular_function | actin filament binding |
A | 0051017 | biological_process | actin filament bundle assembly |
A | 0051491 | biological_process | positive regulation of filopodium assembly |
A | 0070062 | cellular_component | extracellular exosome |
A | 0070161 | cellular_component | anchoring junction |
A | 0071803 | biological_process | positive regulation of podosome assembly |
A | 0090091 | biological_process | positive regulation of extracellular matrix disassembly |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | binding site for residue ACT A 501 |
Chain | Residue |
A | TRP101 |
A | VAL134 |
A | TYR186 |
A | THR213 |
A | LEU214 |
A | H0N507 |
A | HOH717 |
A | HOH842 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue EDO A 502 |
Chain | Residue |
A | ARG100 |
A | SER133 |
A | HOH628 |
A | ASN18 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue EDO A 503 |
Chain | Residue |
A | GLN266 |
A | ALA267 |
A | ALA268 |
A | ARG344 |
A | LEU375 |
A | LEU377 |
A | HOH871 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue EDO A 504 |
Chain | Residue |
A | ALA327 |
A | SER328 |
A | SER329 |
A | ASN331 |
A | ASP372 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue EDO A 505 |
Chain | Residue |
A | ARG118 |
A | THR401 |
A | HOH766 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue EDO A 506 |
Chain | Residue |
A | LEU380 |
A | ILE381 |
A | ASN382 |
A | ARG383 |
A | PRO384 |
A | PHE418 |
site_id | AC7 |
Number of Residues | 15 |
Details | binding site for residue H0N A 507 |
Chain | Residue |
A | LEU48 |
A | ALA58 |
A | ILE93 |
A | TRP101 |
A | VAL134 |
A | LEU214 |
A | GLU215 |
A | PHE216 |
A | ARG217 |
A | GLN277 |
A | ACT501 |
A | HOH722 |
A | HOH755 |
A | HOH800 |
A | HOH877 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylthreonine => ECO:0000269|Ref.9, ECO:0007744|PubMed:22223895 |
Chain | Residue | Details |
A | THR2 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648 |
Chain | Residue | Details |
A | SER38 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:8999969, ECO:0000305|PubMed:22155786 |
Chain | Residue | Details |
A | SER39 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q61553 |
Chain | Residue | Details |
A | LYS74 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER127 | |
A | SER234 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | THR239 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P85845 |
Chain | Residue | Details |
A | THR403 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447 |
Chain | Residue | Details |
A | LYS399 |