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4GP0

The crystal structure of human fascin 1 R149A K150A R151A mutant

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 Residues3
DetailsBINDING SITE FOR RESIDUE BR A 501
ChainResidue
AGLY86
APRO87
AASP88

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 502
ChainResidue
ATHR484
AVAL485
BARG398

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 503
ChainResidue
BTHR401
ACYS456
AASP457
BVAL400

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 504
ChainResidue
AGLU417
APHE418
AGOL514

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 505
ChainResidue
ASER329
ALYS330

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 506
ChainResidue
AGLN182
AASP183
AARG185

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 507
ChainResidue
APHE418
AASP420

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 508
ChainResidue
AHOH608
BGLN124
BTHR125

site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 509
ChainResidue
AASP446

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 510
ChainResidue
AHIS198
AARG229

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 511
ChainResidue
ALYS131
BARG68

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 512
ChainResidue
ALYS43
AGLN44

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 513
ChainResidue
AASP342
AARG343
AARG344
AILE345
AGLY421
ATYR423
APHE452
APHE453

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 514
ChainResidue
ALEU380
AILE381
AASN382
AARG383
APRO384
ALEU416
APHE418
ACL504

site_idBC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 515
ChainResidue
ACYS260
AALA261
ALEU296
AILE298
ACYS456
AASN459
ALYS460
ATYR493

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 516
ChainResidue
AALA149
AVAL165
AASP166
APRO236

site_idBC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DTT A 517
ChainResidue
AARG341
AASP342
AARG343
AARG344
ALEU375
BHOH693
BHOH694

site_idBC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BR B 501
ChainResidue
BARG167
BASP168

site_idCC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BR B 502
ChainResidue
BARG82
BGLY86
BPRO87
BASP88

site_idCC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BR B 503
ChainResidue
BGLN182
BARG185

site_idCC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BR B 504
ChainResidue
AARG167
AASP168
BARG201

site_idCC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BR B 505
ChainResidue
BTYR230
BLYS244

site_idCC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BR B 506
ChainResidue
BARG90

site_idCC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 507
ChainResidue
ATHR434
AVAL435
AVAL449
BARG110
BGLN124

site_idCC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 508
ChainResidue
BGLU83

site_idCC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 509
ChainResidue
ATHR320
BPHE418
BASP420

site_idCC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 510
ChainResidue
BGLY56
BARG217
BSER218

site_idDC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 511
ChainResidue
BASP199
BARG229

site_idDC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 512
ChainResidue
AARG205

site_idDC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 513
ChainResidue
BGLN104

site_idDC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 514
ChainResidue
BSER409
BHOH622

site_idDC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 515
ChainResidue
BHOH622
BSER409
BSER410

site_idDC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 516
ChainResidue
BALA107
BTHR246
BLYS247
BVAL248

site_idDC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 517
ChainResidue
BLYS131

site_idDC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 518
ChainResidue
BARG185

site_idDC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 519
ChainResidue
BVAL126

site_idEC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 520
ChainResidue
BPHE418
BGOL528

site_idEC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 521
ChainResidue
BARG408

site_idEC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 522
ChainResidue
BASP446

site_idEC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 523
ChainResidue
BLYS22
BTHR115

site_idEC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 524
ChainResidue
BVAL400

site_idEC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 525
ChainResidue
BTRP340
BASP342
BILE345
BGLY421
BTYR423
BPHE452
BPHE453
BHOH604
BHOH631

site_idEC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 526
ChainResidue
BHIS392
BASN407
BARG408
BSER409
BHOH739

site_idEC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 527
ChainResidue
BSER133
BVAL134
BGLN182
BARG185
BHOH695

site_idEC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 528
ChainResidue
BLEU380
BILE381
BASN382
BARG383
BPRO384
BLEU416
BPHE418
BCL520
BGOL529

site_idFC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 529
ChainResidue
ATHR326
BHIS193
BPRO384
BGLN415
BLEU416
BGLU417
BGOL528

site_idFC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL B 530
ChainResidue
BARG344
BASP420

site_idFC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE DTT B 531
ChainResidue
BLYS41
BLYS42
BLYS43

site_idFC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE DTT B 532
ChainResidue
BGLY113
BGLU130
BHOH633

site_idFC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EPE B 533
ChainResidue
AGLU207
BASP166
BTHR289
BASP290

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

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PDB entries from 2024-11-06

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