3P53
Structure of fascin
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 |
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 | 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 | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 494 |
Chain | Residue |
A | LEU380 |
A | ILE381 |
A | ASN382 |
A | ARG383 |
A | PRO384 |
A | LEU416 |
A | PHE418 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 495 |
Chain | Residue |
A | GLY421 |
A | TYR423 |
A | PHE452 |
A | PHE453 |
A | ASP342 |
A | MET378 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 496 |
Chain | Residue |
A | LYS32 |
A | VAL33 |
A | VAL78 |
A | ASP117 |
A | ARG118 |
A | LEU119 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 497 |
Chain | Residue |
A | LYS304 |
A | ASP337 |
A | ARG348 |
A | ALA349 |
A | SER350 |
B | ASP446 |
site_id | AC5 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE 12P A 498 |
Chain | Residue |
A | ILE17 |
A | ASN18 |
A | CYS19 |
A | ASP98 |
A | ARG100 |
A | PRO128 |
A | LYS131 |
A | SER133 |
A | PHE181 |
A | ASP183 |
A | GLN184 |
A | ARG185 |
A | TYR186 |
A | HOH633 |
B | PHE31 |
B | ARG68 |
B | GLU81 |
B | GLU83 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE 1PE A 499 |
Chain | Residue |
A | THR318 |
A | ALA319 |
A | THR320 |
A | ASN351 |
A | LYS353 |
A | SER366 |
A | HOH658 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE 1PE A 500 |
Chain | Residue |
A | ARG389 |
A | GLY390 |
A | LYS460 |
A | PRO487 |
A | LEU490 |
A | GLU492 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 1PE A 501 |
Chain | Residue |
A | LEU40 |
A | LYS42 |
A | ILE45 |
A | ALA137 |
A | ARG389 |
A | GLY390 |
A | GLU391 |
A | HIS392 |
A | GLY393 |
site_id | AC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 495 |
Chain | Residue |
B | LEU380 |
B | ILE381 |
B | ASN382 |
B | ARG383 |
B | PRO384 |
B | LEU416 |
B | PHE418 |
B | HOH591 |
site_id | BC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL B 496 |
Chain | Residue |
B | ASP342 |
B | ARG343 |
B | ARG344 |
B | ILE345 |
B | GLY421 |
B | TYR423 |
B | PHE452 |
B | PHE453 |
B | HOH533 |
B | HOH557 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 497 |
Chain | Residue |
B | LYS32 |
B | VAL33 |
B | ASP117 |
B | ARG118 |
B | LEU119 |
B | HOH614 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 498 |
Chain | Residue |
A | LYS74 |
A | ASP75 |
A | ARG110 |
B | PRO448 |
B | VAL449 |
B | ASP450 |
B | HOH556 |
site_id | BC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 1PE B 494 |
Chain | Residue |
B | LYS460 |
B | PRO487 |
B | LEU490 |
B | GLU492 |
B | HOH663 |
B | HOH667 |
B | ARG389 |
B | GLY390 |
B | GLU391 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE 1PE B 499 |
Chain | Residue |
B | HIS135 |
B | SER410 |
B | HOH659 |
B | HOH679 |
site_id | BC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PG0 B 500 |
Chain | Residue |
B | LEU40 |
B | LYS41 |
B | ALA137 |
B | ARG389 |
B | HIS392 |
B | PHE394 |
B | ASN407 |
B | ARG408 |
B | SER409 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylthreonine => ECO:0000269|Ref.9, ECO:0007744|PubMed:22223895 |
Chain | Residue | Details |
A | THR2 | |
B | THR2 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648 |
Chain | Residue | Details |
A | SER38 | |
B | SER38 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:8999969, ECO:0000305|PubMed:22155786 |
Chain | Residue | Details |
A | SER39 | |
B | SER39 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q61553 |
Chain | Residue | Details |
A | LYS74 | |
B | LYS74 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER127 | |
A | SER234 | |
B | SER127 | |
B | SER234 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | THR239 | |
B | THR239 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P85845 |
Chain | Residue | Details |
A | THR403 | |
B | THR403 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447 |
Chain | Residue | Details |
A | LYS399 | |
B | LYS399 |