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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

2A40

Ternary complex of the WH2 domain of WAVE with Actin-DNAse I

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
B0002283biological_processneutrophil activation involved in immune response
B0002673biological_processregulation of acute inflammatory response
B0003677molecular_functionDNA binding
B0003779molecular_functionactin binding
B0003824molecular_functioncatalytic activity
B0004518molecular_functionnuclease activity
B0004519molecular_functionendonuclease activity
B0004530molecular_functiondeoxyribonuclease I activity
B0004536molecular_functionDNA nuclease activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005635cellular_componentnuclear envelope
B0006308biological_processDNA catabolic process
B0006915biological_processapoptotic process
B0016787molecular_functionhydrolase activity
B0031410cellular_componentcytoplasmic vesicle
B0042588cellular_componentzymogen granule
B0070948biological_processregulation of neutrophil mediated cytotoxicity
C0003779molecular_functionactin binding
D0000166molecular_functionnucleotide binding
D0000287molecular_functionmagnesium ion binding
D0001725cellular_componentstress fiber
D0003785molecular_functionactin monomer binding
D0005509molecular_functioncalcium ion binding
D0005515molecular_functionprotein binding
D0005523molecular_functiontropomyosin binding
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005856cellular_componentcytoskeleton
D0005865cellular_componentstriated muscle thin filament
D0005884cellular_componentactin filament
D0010628biological_processpositive regulation of gene expression
D0016787molecular_functionhydrolase activity
D0019904molecular_functionprotein domain specific binding
D0030027cellular_componentlamellipodium
D0030041biological_processactin filament polymerization
D0030175cellular_componentfilopodium
D0030240biological_processskeletal muscle thin filament assembly
D0031013molecular_functiontroponin I binding
D0031432molecular_functiontitin binding
D0031941cellular_componentfilamentous actin
D0032036molecular_functionmyosin heavy chain binding
D0032432cellular_componentactin filament bundle
D0042802molecular_functionidentical protein binding
D0044297cellular_componentcell body
D0048306molecular_functioncalcium-dependent protein binding
D0048741biological_processskeletal muscle fiber development
D0051017biological_processactin filament bundle assembly
D0090131biological_processmesenchyme migration
D0098723cellular_componentskeletal muscle myofibril
D0140660molecular_functioncytoskeletal motor activator activity
E0002283biological_processneutrophil activation involved in immune response
E0002673biological_processregulation of acute inflammatory response
E0003677molecular_functionDNA binding
E0003779molecular_functionactin binding
E0003824molecular_functioncatalytic activity
E0004518molecular_functionnuclease activity
E0004519molecular_functionendonuclease activity
E0004530molecular_functiondeoxyribonuclease I activity
E0004536molecular_functionDNA nuclease activity
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0005634cellular_componentnucleus
E0005635cellular_componentnuclear envelope
E0006308biological_processDNA catabolic process
E0006915biological_processapoptotic process
E0016787molecular_functionhydrolase activity
E0031410cellular_componentcytoplasmic vesicle
E0042588cellular_componentzymogen granule
E0070948biological_processregulation of neutrophil mediated cytotoxicity
F0003779molecular_functionactin binding
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_idPS00918
Number of Residues8
DetailsDNASE_I_2 Deoxyribonuclease I signature 2. GDFNAdCS
ChainResidueDetails
BGLY167-SER174
site_idPS00919
Number of Residues21
DetailsDNASE_I_1 Deoxyribonuclease I signature 1. IVALHSAPsdavaEINsLyDV
ChainResidueDetails
BILE130-VAL150
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 Residues26
DetailsRegion: {"description":"Interaction with alpha-actinin","evidences":[{"source":"PubMed","id":"8449927","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsModified residue: {"description":"Methionine (R)-sulfoxide","evidences":[{"source":"UniProtKB","id":"P68134","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues2
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 Residues2
DetailsModified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"ADP-ribosylarginine; by SpvB","evidences":[{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"2395459","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"2395459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"4976790","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues4
DetailsSite: {"description":"Involved in actin-binding","evidences":[{"source":"PubMed","id":"2395459","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsSite: {"description":"Nitration by tetranitromethane destroys a Ca(2+) binding site and inactivates enzyme"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"1748997","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3560229","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues34
DetailsDomain: {"description":"WH2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00406","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1dnk
ChainResidueDetails
BASP212
BHIS134
BGLU78
BHIS252
site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1dnk
ChainResidueDetails
EASP212
EHIS134
EGLU78
EHIS252
site_idMCSA1
Number of Residues7
DetailsM-CSA 41
ChainResidueDetails
BGLU39metal ligand
BTYR76electrostatic stabiliser
BGLU78electrostatic stabiliser, increase acidity, increase basicity
BHIS134proton acceptor, proton donor
BASP168metal ligand
BASP212electrostatic stabiliser, increase acidity, increase basicity
BHIS252proton acceptor, proton donor
site_idMCSA2
Number of Residues7
DetailsM-CSA 41
ChainResidueDetails
EGLU39metal ligand
ETYR76electrostatic stabiliser
EGLU78electrostatic stabiliser, increase acidity, increase basicity
EHIS134proton acceptor, proton donor
EASP168metal ligand
EASP212electrostatic stabiliser, increase acidity, increase basicity
EHIS252proton acceptor, proton donor

246031

PDB entries from 2025-12-10

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