4GOV
The crystal structure of human fascin 1 S39D 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 | 1 |
| Details | BINDING SITE FOR RESIDUE BR A 501 |
| Chain | Residue |
| A | ALA370 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BR A 502 |
| Chain | Residue |
| A | ARG82 |
| A | GLY86 |
| A | ASP88 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 503 |
| Chain | Residue |
| A | ARG118 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 504 |
| Chain | Residue |
| A | ARG82 |
| A | GLU83 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 505 |
| Chain | Residue |
| B | LYS32 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 506 |
| Chain | Residue |
| A | ASP168 |
| A | VAL169 |
| A | ARG167 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 507 |
| Chain | Residue |
| A | PRO52 |
| A | ARG90 |
| A | HOH628 |
| A | HOH633 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 508 |
| Chain | Residue |
| A | TRP340 |
| A | ASP342 |
| A | ILE345 |
| A | GLY421 |
| A | TYR423 |
| A | PHE452 |
| A | PHE453 |
| A | HOH641 |
| A | HOH677 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 509 |
| Chain | Residue |
| A | LYS379 |
| A | LEU380 |
| A | ILE381 |
| A | ASN382 |
| A | ARG383 |
| A | PRO384 |
| A | LEU416 |
| A | PHE418 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 510 |
| Chain | Residue |
| A | TYR145 |
| A | VAL147 |
| A | LYS150 |
| A | LYS220 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE DTT A 511 |
| Chain | Residue |
| A | SER57 |
| A | ALA58 |
| A | ARG217 |
| A | SER218 |
| A | GLY219 |
| A | LYS220 |
| A | LEU253 |
| A | HOH742 |
| A | HOH775 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BR B 501 |
| Chain | Residue |
| B | ARG82 |
| B | GLY86 |
| B | ASP88 |
| site_id | BC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE BR B 502 |
| Chain | Residue |
| B | ARG90 |
| site_id | BC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE BR B 503 |
| Chain | Residue |
| B | GLU83 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BR B 504 |
| Chain | Residue |
| B | ARG217 |
| B | SER218 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 505 |
| Chain | Residue |
| A | THR320 |
| B | ASP420 |
| site_id | BC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 506 |
| Chain | Residue |
| B | PRO128 |
| B | LYS131 |
| site_id | BC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 507 |
| Chain | Residue |
| B | ARG167 |
| B | ASP168 |
| site_id | CC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 508 |
| Chain | Residue |
| A | GLN324 |
| B | PHE418 |
| site_id | CC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 509 |
| Chain | Residue |
| B | GLN182 |
| B | ARG185 |
| B | HOH648 |
| site_id | CC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 510 |
| Chain | Residue |
| B | TYR230 |
| B | GLY243 |
| B | LYS244 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 511 |
| Chain | Residue |
| A | THR434 |
| A | VAL435 |
| A | VAL449 |
| B | ARG110 |
| B | GLN124 |
| site_id | CC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 512 |
| Chain | Residue |
| B | THR115 |
| B | GLU116 |
| site_id | CC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 513 |
| Chain | Residue |
| B | TRP340 |
| B | ASP342 |
| B | ILE345 |
| B | GLY421 |
| B | TYR423 |
| B | PHE452 |
| B | PHE453 |
| B | HOH863 |
| site_id | CC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 514 |
| Chain | Residue |
| B | LEU380 |
| B | ILE381 |
| B | ASN382 |
| B | ARG383 |
| B | PRO384 |
| B | LEU416 |
| B | PHE418 |
| B | HOH621 |
| site_id | CC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 515 |
| Chain | Residue |
| A | THR326 |
| A | ALA327 |
| A | SER329 |
| A | HOH638 |
| B | GLN415 |
| B | LYS426 |
| B | SER428 |
| B | GLY430 |
| site_id | CC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 516 |
| Chain | Residue |
| A | HOH869 |
| B | ASN21 |
| A | LYS43 |
| A | HIS65 |
| site_id | DC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 517 |
| Chain | Residue |
| B | GLU8 |
| B | ALA9 |
| B | GLN11 |
| B | GLN258 |
| B | GLU492 |
| B | HOH789 |
| site_id | DC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 518 |
| Chain | Residue |
| A | PRO487 |
| B | ARG398 |
| B | LYS399 |
| B | VAL400 |
| B | ARG408 |
| site_id | DC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL B 519 |
| Chain | Residue |
| B | ARG344 |
| B | ASP420 |
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 | ASP39 | |
| B | ASP39 |
| 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 |
