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3CJC

Actin dimer cross-linked by V. cholerae MARTX toxin and complexed with DNase I and Gelsolin-segment 1

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
D0002283biological_processneutrophil activation involved in immune response
D0002673biological_processregulation of acute inflammatory response
D0003677molecular_functionDNA binding
D0003779molecular_functionactin binding
D0003824molecular_functioncatalytic activity
D0004519molecular_functionendonuclease activity
D0004530molecular_functiondeoxyribonuclease I activity
D0004536molecular_functionDNA nuclease activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005634cellular_componentnucleus
D0005635cellular_componentnuclear envelope
D0006308biological_processDNA catabolic process
D0006915biological_processapoptotic process
D0031410cellular_componentcytoplasmic vesicle
D0042588cellular_componentzymogen granule
D0070948biological_processregulation of neutrophil mediated cytotoxicity
G0051015molecular_functionactin filament 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
DGLY167-SER174

site_idPS00919
Number of Residues21
DetailsDNASE_I_1 Deoxyribonuclease I signature 1. IVALHSAPsdavaEINsLyDV
ChainResidueDetails
DILE130-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 Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:19666512, ECO:0007744|PDB:3FFK
ChainResidueDetails
GGLY41
GASP42
GGLU73
GASP85
GGLY90
GALA92
GVAL121

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
GLYS111

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by SRC; in vitro => ECO:0000269|PubMed:10210201
ChainResidueDetails
GTYR35
DVAL67

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Nitration by tetranitromethane destroys a Ca(2+) binding site and inactivates enzyme
ChainResidueDetails
DTYR65

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:1748997, ECO:0000269|PubMed:3560229
ChainResidueDetails
DASN18

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133
ChainResidueDetails
ALYS84

site_idSWS_FT_FI7
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
DGLU39metal ligand
DTYR76electrostatic stabiliser
DGLU78electrostatic stabiliser, increase acidity, increase basicity
DHIS134proton acceptor, proton donor
DASP168metal ligand
DASP212electrostatic stabiliser, increase acidity, increase basicity
DHIS252proton acceptor, proton donor

227111

PDB entries from 2024-11-06

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