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2A3Z

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

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
B0002283biological_processneutrophil activation involved in immune response
B0002673biological_processregulation of acute inflammatory response
B0003677molecular_functionDNA binding
B0003779molecular_functionactin binding
B0003824molecular_functioncatalytic 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
B0031410cellular_componentcytoplasmic vesicle
B0042588cellular_componentzymogen granule
B0070948biological_processregulation of neutrophil mediated cytotoxicity
C0003779molecular_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 Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:2395459
ChainResidueDetails
BGLU78

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:2395459, ECO:0000269|PubMed:4976790
ChainResidueDetails
BHIS134
AMET47

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Involved in actin-binding => ECO:0000269|PubMed:2395459
ChainResidueDetails
BGLU13
BVAL67

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Nitration by tetranitromethane destroys a Ca(2+) binding site and inactivates enzyme
ChainResidueDetails
BTYR65

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:1748997, ECO:0000269|PubMed:3560229
ChainResidueDetails
BASN18

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096
ChainResidueDetails
AARG177

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1dnk
ChainResidueDetails
BASP212
BHIS134
BGLU78
BHIS252

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

227561

PDB entries from 2024-11-20

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