6I15
CRYSTAL STRUCTURE OF FASCIN IN COMPLEX WITH COMPOUND 11
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 | 0031252 | cellular_component | cell leading edge |
| 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 | 6 |
| Details | binding site for residue EDO A 501 |
| Chain | Residue |
| A | ILE17 |
| A | ASN18 |
| A | ASN21 |
| A | ARG100 |
| A | SER133 |
| A | HOH683 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 502 |
| Chain | Residue |
| A | HOH717 |
| A | VAL134 |
| A | THR213 |
| A | LEU214 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 503 |
| Chain | Residue |
| A | VAL169 |
| A | TRP171 |
| A | ARG308 |
| A | THR309 |
| A | GLY312 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue GZT A 504 |
| Chain | Residue |
| A | LEU16 |
| A | LEU48 |
| A | ILE93 |
| A | TRP101 |
| A | LEU103 |
| A | VAL134 |
| A | LEU214 |
| A | GLU215 |
| A | PHE216 |
| A | ARG217 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by PKC","evidences":[{"source":"PubMed","id":"8999969","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22155786","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q61553","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P85845","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"25218447","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
