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6I11

CRYSTAL STRUCTURE OF FASCIN IN COMPLEX WITH COMPOUND 3

Functional Information from GO Data
ChainGOidnamespacecontents
A0001725cellular_componentstress fiber
A0001726cellular_componentruffle
A0002102cellular_componentpodosome
A0003723molecular_functionRNA binding
A0003779molecular_functionactin binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005902cellular_componentmicrovillus
A0005911cellular_componentcell-cell junction
A0005938cellular_componentcell cortex
A0007015biological_processactin filament organization
A0007043biological_processcell-cell junction assembly
A0007163biological_processestablishment or maintenance of cell polarity
A0008144molecular_functionobsolete drug binding
A0010592biological_processpositive regulation of lamellipodium assembly
A0015629cellular_componentactin cytoskeleton
A0016477biological_processcell migration
A0030027cellular_componentlamellipodium
A0030035biological_processmicrospike assembly
A0030036biological_processactin cytoskeleton organization
A0030046biological_processparallel actin filament bundle assembly
A0030175cellular_componentfilopodium
A0030426cellular_componentgrowth cone
A0030674molecular_functionprotein-macromolecule adaptor activity
A0031253cellular_componentcell projection membrane
A0032534biological_processregulation of microvillus assembly
A0032956biological_processregulation of actin cytoskeleton organization
A0035089biological_processestablishment of apical/basal cell polarity
A0042995cellular_componentcell projection
A0044393cellular_componentmicrospike
A0045296molecular_functioncadherin binding
A0048870biological_processcell motility
A0051015molecular_functionactin filament binding
A0051017biological_processactin filament bundle assembly
A0051491biological_processpositive regulation of filopodium assembly
A0070062cellular_componentextracellular exosome
A0070161cellular_componentanchoring junction
A0071803biological_processpositive regulation of podosome assembly
A0090091biological_processpositive regulation of extracellular matrix disassembly
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ACT A 501
ChainResidue
ATRP101
AVAL134
ATHR213
ALEU214
AHOH621

site_idAC2
Number of Residues9
Detailsbinding site for residue H0H A 502
ChainResidue
AVAL134
ALEU214
AGLU215
APHE216
AHOH797
ALEU48
AILE93
AALA95
ATRP101

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylthreonine => ECO:0000269|Ref.9, ECO:0007744|PubMed:22223895
ChainResidueDetails
ATHR2

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER38

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:8999969, ECO:0000305|PubMed:22155786
ChainResidueDetails
ASER39

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q61553
ChainResidueDetails
ALYS74

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER127
ASER234

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR239

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P85845
ChainResidueDetails
ATHR403

site_idSWS_FT_FI8
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447
ChainResidueDetails
ALYS399

218853

PDB entries from 2024-04-24

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