Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3TU5

Actin complex with Gelsolin Segment 1 fused to Cobl segment

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
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 Residues25
DetailsRegion: {"description":"Interaction with alpha-actinin","evidences":[{"source":"PubMed","id":"8449927","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"Methionine (R)-sulfoxide","evidences":[{"source":"UniProtKB","id":"P68134","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"PubMed","id":"1150665","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"213279","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2395459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"499690","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ATN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NWK","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"ADP-ribosylarginine; by SpvB","evidences":[{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues82
DetailsRepeat: {"description":"Gelsolin-like 1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues123
DetailsRegion: {"description":"Actin-severing","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues3
DetailsRegion: {"description":"Actin-actin interfilament contact point"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19666512","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FFK","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues7
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by SRC; in vitro","evidences":[{"source":"PubMed","id":"10210201","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

PDB statisticsPDBj update infoContact PDBjnumon