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2A41

Ternary complex of the WH2 Domain of WIP 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
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_idPS01132
Number of Residues13
DetailsACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR
ChainResidueDetails
ALEU104-ARG116

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Asymmetric dimethylarginine => ECO:0000250|UniProtKB:Q8K1I7
ChainResidueDetails
CARG33

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
BVAL67
BGLU13

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_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

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PDB entries from 2024-04-17

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