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3LLP

1.8 Angstrom human fascin 1 crystal structure

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
B0001725cellular_componentstress fiber
B0001726cellular_componentruffle
B0002102cellular_componentpodosome
B0003723molecular_functionRNA binding
B0003779molecular_functionactin binding
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005902cellular_componentmicrovillus
B0005911cellular_componentcell-cell junction
B0005938cellular_componentcell cortex
B0007015biological_processactin filament organization
B0007043biological_processcell-cell junction assembly
B0007163biological_processestablishment or maintenance of cell polarity
B0008144molecular_functionobsolete drug binding
B0010592biological_processpositive regulation of lamellipodium assembly
B0015629cellular_componentactin cytoskeleton
B0016477biological_processcell migration
B0030027cellular_componentlamellipodium
B0030035biological_processmicrospike assembly
B0030036biological_processactin cytoskeleton organization
B0030046biological_processparallel actin filament bundle assembly
B0030175cellular_componentfilopodium
B0030426cellular_componentgrowth cone
B0030674molecular_functionprotein-macromolecule adaptor activity
B0031253cellular_componentcell projection membrane
B0032534biological_processregulation of microvillus assembly
B0032956biological_processregulation of actin cytoskeleton organization
B0035089biological_processestablishment of apical/basal cell polarity
B0042995cellular_componentcell projection
B0044393cellular_componentmicrospike
B0045296molecular_functioncadherin binding
B0048870biological_processcell motility
B0051015molecular_functionactin filament binding
B0051017biological_processactin filament bundle assembly
B0051491biological_processpositive regulation of filopodium assembly
B0070062cellular_componentextracellular exosome
B0070161cellular_componentanchoring junction
B0071803biological_processpositive regulation of podosome assembly
B0090091biological_processpositive regulation of extracellular matrix disassembly
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 494
ChainResidue
ACYS260
AHOH661
AALA261
ALEU296
ACYS456
AASP457
ATYR458
AASN459
ALYS460
ATYR493

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 495
ChainResidue
ALEU380
AILE381
AASN382
AARG383
APRO384
ALEU416
APHE418
AHOH956

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 496
ChainResidue
AASP342
AARG344
AILE345
AGLY421
ATYR423
APHE452
APHE453
AHOH529
AHOH1052

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 497
ChainResidue
AHIS139
AGLN141
AGLN258
ATYR493
AHOH659

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BR A 498
ChainResidue
AGLY86
AASP88

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BR A 499
ChainResidue
AARG167
AASP168
BARG201

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BR A 500
ChainResidue
AGLN182
AARG185

site_idAC8
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL B 494
ChainResidue
BASP342
BARG343
BARG344
BILE345
BGLY421
BTYR423
BPHE452
BPHE453
BHOH516
BHOH535

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 495
ChainResidue
BLYS379
BLEU380
BILE381
BASN382
BARG383
BPRO384
BLEU416
BPHE418

site_idBC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE EPE B 496
ChainResidue
AARG201
AGLU207
AHOH533
BASP166
BARG167
BTHR289
BASP290
BGLN291
BSO4500
BHOH538

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K B 497
ChainResidue
AASP192
AHOH664
BTHR275
BARG276
BGLY278
BHOH599

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 498
ChainResidue
AARG205
BARG308
BGLY312
BHOH587
BHOH1058

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 499
ChainResidue
BARG82
BGLU83
BVAL84

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 500
ChainResidue
APRO208
BARG151
BASP166
BASP168
BEPE496
BHOH538
BHOH638
BHOH666

site_idBC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BR B 501
ChainResidue
BARG167
BASP168

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BR B 502
ChainResidue
BARG82
BGLY86
BASP88

site_idBC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BR B 503
ChainResidue
BTYR230
BLYS244

site_idBC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BR B 504
ChainResidue
BGLN182
BGLN184
BARG185

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N-acetylthreonine => ECO:0000269|Ref.9, ECO:0007744|PubMed:22223895
ChainResidueDetails
ATHR2
BTHR2

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER38
BSER38

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:8999969, ECO:0000305|PubMed:22155786
ChainResidueDetails
ASER39
BSER39

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q61553
ChainResidueDetails
ALYS74
BLYS74

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER127
ASER234
BSER127
BSER234

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR239
BTHR239

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P85845
ChainResidueDetails
ATHR403
BTHR403

site_idSWS_FT_FI8
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447
ChainResidueDetails
ALYS399
BLYS399

221051

PDB entries from 2024-06-12

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