Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

8BJH

chimera of the inactive ExoY Nucleotidyl Cyclase domain from Vibrio nigripulchritudo MARTX toxin, with the double mutation K3528M and K3535I, fused to a proline-Rich-Domain (PRD) and profilin, bound to Latrunculin B-ADP-Mg-actin

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
B0000774molecular_functionadenyl-nucleotide exchange factor activity
B0001784molecular_functionphosphotyrosine residue binding
B0001843biological_processneural tube closure
B0003723molecular_functionRNA binding
B0003779molecular_functionactin binding
B0003785molecular_functionactin monomer binding
B0005515molecular_functionprotein binding
B0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005925cellular_componentfocal adhesion
B0005938cellular_componentcell cortex
B0006357biological_processregulation of transcription by RNA polymerase II
B0008294molecular_functioncalcium- and calmodulin-responsive adenylate cyclase activity
B0010634biological_processpositive regulation of epithelial cell migration
B0016020cellular_componentmembrane
B0030036biological_processactin cytoskeleton organization
B0030833biological_processregulation of actin filament polymerization
B0030837biological_processnegative regulation of actin filament polymerization
B0030838biological_processpositive regulation of actin filament polymerization
B0031267molecular_functionsmall GTPase binding
B0032232biological_processnegative regulation of actin filament bundle assembly
B0032233biological_processpositive regulation of actin filament bundle assembly
B0032781biological_processpositive regulation of ATP-dependent activity
B0044087biological_processregulation of cellular component biogenesis
B0045296molecular_functioncadherin binding
B0050804biological_processmodulation of chemical synaptic transmission
B0050821biological_processprotein stabilization
B0051497biological_processnegative regulation of stress fiber assembly
B0060074biological_processsynapse maturation
B0070062cellular_componentextracellular exosome
B0070064molecular_functionproline-rich region binding
B0072562cellular_componentblood microparticle
B0098885biological_processmodification of postsynaptic actin cytoskeleton
B0098978cellular_componentglutamatergic synapse
B0110053biological_processregulation of actin filament organization
B1900029biological_processpositive regulation of ruffle assembly
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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:3342873, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712
ChainResidueDetails
BALA903

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P62963
ChainResidueDetails
BSER929
AMET47

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER958

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332
ChainResidueDetails
BSER986

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS1006
BLYS1009

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
BTYR1030

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine; by ROCK1 => ECO:0000269|PubMed:18573880
ChainResidueDetails
BSER1039

site_idSWS_FT_FI8
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
ChainResidueDetails
BLYS955

224572

PDB entries from 2024-09-04

PDB statisticsPDBj update infoContact PDBjnumon