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3TU5

Actin complex with Gelsolin Segment 1 fused to Cobl segment

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0001725cellular_componentstress fiber
A0003785molecular_functionactin monomer binding
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005523molecular_functiontropomyosin binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005865cellular_componentstriated muscle thin filament
A0005884cellular_componentactin filament
A0010628biological_processpositive regulation of gene expression
A0016787molecular_functionhydrolase activity
A0019904molecular_functionprotein domain specific binding
A0030027cellular_componentlamellipodium
A0030041biological_processactin filament polymerization
A0030175cellular_componentfilopodium
A0030240biological_processskeletal muscle thin filament assembly
A0031013molecular_functiontroponin I binding
A0031432molecular_functiontitin binding
A0031941cellular_componentfilamentous actin
A0032036molecular_functionmyosin heavy chain binding
A0032432cellular_componentactin filament bundle
A0042802molecular_functionidentical protein binding
A0044297cellular_componentcell body
A0048306molecular_functioncalcium-dependent protein binding
A0048741biological_processskeletal muscle fiber development
A0051017biological_processactin filament bundle assembly
A0090131biological_processmesenchyme migration
A0098723cellular_componentskeletal muscle myofibril
A0140660molecular_functioncytoskeletal motor activator activity
B0003779molecular_functionactin binding
B0003785molecular_functionactin monomer binding
B0007015biological_processactin filament organization
B0051015molecular_functionactin filament binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 376
ChainResidue
AATP377
AHOH397
AHOH398

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE ATP A 377
ChainResidue
AASP157
AGLY158
AVAL159
AGLY182
AARG210
ALYS213
AGLU214
AGLY301
AGLY302
ATHR303
AMET305
ALYS336
ACA376
AHOH396
AHOH397
AHOH401
AGLY13
ASER14
AGLY15
ALEU16
ALYS18
AGLY156

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 326
ChainResidue
BGLY41
BASP42
BGLU73
BVAL121

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD A 378
ChainResidue
ATYR133
AALA135
AILE136
AGLY168
ATYR169
AMPD379

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 379
ChainResidue
ATYR169
AMET355
AMPD378
BVAL82
BGLN83

Functional Information from PROSITE/UniProt
site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. YVGDEAQs.KRG
ChainResidueDetails
ATYR53-GLY63

site_idPS00432
Number of Residues9
DetailsACTINS_2 Actins signature 2. WITKqEYDE
ChainResidueDetails
ATRP356-GLU364

site_idPS00500
Number of Residues12
DetailsTHYMOSIN_B4 Thymosin beta-4 family signature. LRKTETqeKNPL
ChainResidueDetails
BLEU253-LEU264

site_idPS01132
Number of Residues13
DetailsACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR
ChainResidueDetails
ALEU104-ARG116

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:19666512, ECO:0007744|PDB:3FFK
ChainResidueDetails
BGLY41
BASP42
BGLU73
BASP85
BGLY90
BALA92
BVAL121

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
BLYS111

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by SRC; in vitro => ECO:0000269|PubMed:10210201
ChainResidueDetails
BTYR35
AMET47

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O75128
ChainResidueDetails
BASP242

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BTHR258
BTHR269

site_idSWS_FT_FI6
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS261
BLYS267
BLYS274

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER266

224931

PDB entries from 2024-09-11

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