3LLP
1.8 Angstrom human fascin 1 crystal structure
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 |
| B | 0001725 | cellular_component | stress fiber |
| B | 0001726 | cellular_component | ruffle |
| B | 0002102 | cellular_component | podosome |
| B | 0003723 | molecular_function | RNA binding |
| B | 0003779 | molecular_function | actin binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005856 | cellular_component | cytoskeleton |
| B | 0005902 | cellular_component | microvillus |
| B | 0005911 | cellular_component | cell-cell junction |
| B | 0005938 | cellular_component | cell cortex |
| B | 0007015 | biological_process | actin filament organization |
| B | 0007043 | biological_process | cell-cell junction assembly |
| B | 0007163 | biological_process | establishment or maintenance of cell polarity |
| B | 0008144 | molecular_function | obsolete drug binding |
| B | 0010592 | biological_process | positive regulation of lamellipodium assembly |
| B | 0015629 | cellular_component | actin cytoskeleton |
| B | 0016477 | biological_process | cell migration |
| B | 0030027 | cellular_component | lamellipodium |
| B | 0030035 | biological_process | microspike assembly |
| B | 0030036 | biological_process | actin cytoskeleton organization |
| B | 0030046 | biological_process | parallel actin filament bundle assembly |
| B | 0030175 | cellular_component | filopodium |
| B | 0030426 | cellular_component | growth cone |
| B | 0030674 | molecular_function | protein-macromolecule adaptor activity |
| B | 0031252 | cellular_component | cell leading edge |
| B | 0031253 | cellular_component | cell projection membrane |
| B | 0032534 | biological_process | regulation of microvillus assembly |
| B | 0032956 | biological_process | regulation of actin cytoskeleton organization |
| B | 0035089 | biological_process | establishment of apical/basal cell polarity |
| B | 0042995 | cellular_component | cell projection |
| B | 0044393 | cellular_component | microspike |
| B | 0045296 | molecular_function | cadherin binding |
| B | 0048870 | biological_process | cell motility |
| B | 0051015 | molecular_function | actin filament binding |
| B | 0051017 | biological_process | actin filament bundle assembly |
| B | 0051491 | biological_process | positive regulation of filopodium assembly |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0070161 | cellular_component | anchoring junction |
| B | 0071803 | biological_process | positive regulation of podosome assembly |
| B | 0090091 | biological_process | positive regulation of extracellular matrix disassembly |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 494 |
| Chain | Residue |
| A | CYS260 |
| A | HOH661 |
| A | ALA261 |
| A | LEU296 |
| A | CYS456 |
| A | ASP457 |
| A | TYR458 |
| A | ASN459 |
| A | LYS460 |
| A | TYR493 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 495 |
| Chain | Residue |
| A | LEU380 |
| A | ILE381 |
| A | ASN382 |
| A | ARG383 |
| A | PRO384 |
| A | LEU416 |
| A | PHE418 |
| A | HOH956 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 496 |
| Chain | Residue |
| A | ASP342 |
| A | ARG344 |
| A | ILE345 |
| A | GLY421 |
| A | TYR423 |
| A | PHE452 |
| A | PHE453 |
| A | HOH529 |
| A | HOH1052 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 497 |
| Chain | Residue |
| A | HIS139 |
| A | GLN141 |
| A | GLN258 |
| A | TYR493 |
| A | HOH659 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BR A 498 |
| Chain | Residue |
| A | GLY86 |
| A | ASP88 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BR A 499 |
| Chain | Residue |
| A | ARG167 |
| A | ASP168 |
| B | ARG201 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BR A 500 |
| Chain | Residue |
| A | GLN182 |
| A | ARG185 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 494 |
| Chain | Residue |
| B | ASP342 |
| B | ARG343 |
| B | ARG344 |
| B | ILE345 |
| B | GLY421 |
| B | TYR423 |
| B | PHE452 |
| B | PHE453 |
| B | HOH516 |
| B | HOH535 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 495 |
| Chain | Residue |
| B | LYS379 |
| B | LEU380 |
| B | ILE381 |
| B | ASN382 |
| B | ARG383 |
| B | PRO384 |
| B | LEU416 |
| B | PHE418 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE EPE B 496 |
| Chain | Residue |
| A | ARG201 |
| A | GLU207 |
| A | HOH533 |
| B | ASP166 |
| B | ARG167 |
| B | THR289 |
| B | ASP290 |
| B | GLN291 |
| B | SO4500 |
| B | HOH538 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K B 497 |
| Chain | Residue |
| A | ASP192 |
| A | HOH664 |
| B | THR275 |
| B | ARG276 |
| B | GLY278 |
| B | HOH599 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 498 |
| Chain | Residue |
| A | ARG205 |
| B | ARG308 |
| B | GLY312 |
| B | HOH587 |
| B | HOH1058 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 499 |
| Chain | Residue |
| B | ARG82 |
| B | GLU83 |
| B | VAL84 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 500 |
| Chain | Residue |
| A | PRO208 |
| B | ARG151 |
| B | ASP166 |
| B | ASP168 |
| B | EPE496 |
| B | HOH538 |
| B | HOH638 |
| B | HOH666 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BR B 501 |
| Chain | Residue |
| B | ARG167 |
| B | ASP168 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BR B 502 |
| Chain | Residue |
| B | ARG82 |
| B | GLY86 |
| B | ASP88 |
| site_id | BC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BR B 503 |
| Chain | Residue |
| B | TYR230 |
| B | LYS244 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BR B 504 |
| Chain | Residue |
| B | GLN182 |
| B | GLN184 |
| B | ARG185 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| 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 | 2 |
| 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 | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| 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 |
