4GP0
The crystal structure of human fascin 1 R149A K150A R151A mutant
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 | 3 |
Details | BINDING SITE FOR RESIDUE BR A 501 |
Chain | Residue |
A | GLY86 |
A | PRO87 |
A | ASP88 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 502 |
Chain | Residue |
A | THR484 |
A | VAL485 |
B | ARG398 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 503 |
Chain | Residue |
B | THR401 |
A | CYS456 |
A | ASP457 |
B | VAL400 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 504 |
Chain | Residue |
A | GLU417 |
A | PHE418 |
A | GOL514 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 505 |
Chain | Residue |
A | SER329 |
A | LYS330 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 506 |
Chain | Residue |
A | GLN182 |
A | ASP183 |
A | ARG185 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 507 |
Chain | Residue |
A | PHE418 |
A | ASP420 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 508 |
Chain | Residue |
A | HOH608 |
B | GLN124 |
B | THR125 |
site_id | AC9 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 509 |
Chain | Residue |
A | ASP446 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 510 |
Chain | Residue |
A | HIS198 |
A | ARG229 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 511 |
Chain | Residue |
A | LYS131 |
B | ARG68 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 512 |
Chain | Residue |
A | LYS43 |
A | GLN44 |
site_id | BC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 513 |
Chain | Residue |
A | ASP342 |
A | ARG343 |
A | ARG344 |
A | ILE345 |
A | GLY421 |
A | TYR423 |
A | PHE452 |
A | PHE453 |
site_id | BC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 514 |
Chain | Residue |
A | LEU380 |
A | ILE381 |
A | ASN382 |
A | ARG383 |
A | PRO384 |
A | LEU416 |
A | PHE418 |
A | CL504 |
site_id | BC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 515 |
Chain | Residue |
A | CYS260 |
A | ALA261 |
A | LEU296 |
A | ILE298 |
A | CYS456 |
A | ASN459 |
A | LYS460 |
A | TYR493 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 516 |
Chain | Residue |
A | ALA149 |
A | VAL165 |
A | ASP166 |
A | PRO236 |
site_id | BC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE DTT A 517 |
Chain | Residue |
A | ARG341 |
A | ASP342 |
A | ARG343 |
A | ARG344 |
A | LEU375 |
B | HOH693 |
B | HOH694 |
site_id | BC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE BR B 501 |
Chain | Residue |
B | ARG167 |
B | ASP168 |
site_id | CC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BR B 502 |
Chain | Residue |
B | ARG82 |
B | GLY86 |
B | PRO87 |
B | ASP88 |
site_id | CC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE BR B 503 |
Chain | Residue |
B | GLN182 |
B | ARG185 |
site_id | CC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE BR B 504 |
Chain | Residue |
A | ARG167 |
A | ASP168 |
B | ARG201 |
site_id | CC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE BR B 505 |
Chain | Residue |
B | TYR230 |
B | LYS244 |
site_id | CC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE BR B 506 |
Chain | Residue |
B | ARG90 |
site_id | CC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL B 507 |
Chain | Residue |
A | THR434 |
A | VAL435 |
A | VAL449 |
B | ARG110 |
B | GLN124 |
site_id | CC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL B 508 |
Chain | Residue |
B | GLU83 |
site_id | CC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 509 |
Chain | Residue |
A | THR320 |
B | PHE418 |
B | ASP420 |
site_id | CC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 510 |
Chain | Residue |
B | GLY56 |
B | ARG217 |
B | SER218 |
site_id | DC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL B 511 |
Chain | Residue |
B | ASP199 |
B | ARG229 |
site_id | DC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL B 512 |
Chain | Residue |
A | ARG205 |
site_id | DC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL B 513 |
Chain | Residue |
B | GLN104 |
site_id | DC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL B 514 |
Chain | Residue |
B | SER409 |
B | HOH622 |
site_id | DC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 515 |
Chain | Residue |
B | HOH622 |
B | SER409 |
B | SER410 |
site_id | DC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL B 516 |
Chain | Residue |
B | ALA107 |
B | THR246 |
B | LYS247 |
B | VAL248 |
site_id | DC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL B 517 |
Chain | Residue |
B | LYS131 |
site_id | DC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL B 518 |
Chain | Residue |
B | ARG185 |
site_id | DC9 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL B 519 |
Chain | Residue |
B | VAL126 |
site_id | EC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL B 520 |
Chain | Residue |
B | PHE418 |
B | GOL528 |
site_id | EC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL B 521 |
Chain | Residue |
B | ARG408 |
site_id | EC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL B 522 |
Chain | Residue |
B | ASP446 |
site_id | EC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL B 523 |
Chain | Residue |
B | LYS22 |
B | THR115 |
site_id | EC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL B 524 |
Chain | Residue |
B | VAL400 |
site_id | EC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 525 |
Chain | Residue |
B | TRP340 |
B | ASP342 |
B | ILE345 |
B | GLY421 |
B | TYR423 |
B | PHE452 |
B | PHE453 |
B | HOH604 |
B | HOH631 |
site_id | EC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL B 526 |
Chain | Residue |
B | HIS392 |
B | ASN407 |
B | ARG408 |
B | SER409 |
B | HOH739 |
site_id | EC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL B 527 |
Chain | Residue |
B | SER133 |
B | VAL134 |
B | GLN182 |
B | ARG185 |
B | HOH695 |
site_id | EC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 528 |
Chain | Residue |
B | LEU380 |
B | ILE381 |
B | ASN382 |
B | ARG383 |
B | PRO384 |
B | LEU416 |
B | PHE418 |
B | CL520 |
B | GOL529 |
site_id | FC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 529 |
Chain | Residue |
A | THR326 |
B | HIS193 |
B | PRO384 |
B | GLN415 |
B | LEU416 |
B | GLU417 |
B | GOL528 |
site_id | FC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL B 530 |
Chain | Residue |
B | ARG344 |
B | ASP420 |
site_id | FC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DTT B 531 |
Chain | Residue |
B | LYS41 |
B | LYS42 |
B | LYS43 |
site_id | FC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DTT B 532 |
Chain | Residue |
B | GLY113 |
B | GLU130 |
B | HOH633 |
site_id | FC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EPE B 533 |
Chain | Residue |
A | GLU207 |
B | ASP166 |
B | THR289 |
B | ASP290 |
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 |