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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

5L6W

Structure Of the LIMK1-ATPgammaS-CFL1 Complex

Functional Information from GO Data
ChainGOidnamespacecontents
C0000281biological_processmitotic cytokinesis
C0003779molecular_functionactin binding
C0005102molecular_functionsignaling receptor binding
C0005515molecular_functionprotein binding
C0005615cellular_componentextracellular space
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005856cellular_componentcytoskeleton
C0005911cellular_componentcell-cell junction
C0005925cellular_componentfocal adhesion
C0006606biological_processprotein import into nucleus
C0007162biological_processnegative regulation of cell adhesion
C0007266biological_processRho protein signal transduction
C0008154biological_processactin polymerization or depolymerization
C0009615biological_processresponse to virus
C0010592biological_processpositive regulation of lamellipodium assembly
C0010593biological_processnegative regulation of lamellipodium assembly
C0014823biological_processresponse to activity
C0015629cellular_componentactin cytoskeleton
C0016020cellular_componentmembrane
C0016363cellular_componentnuclear matrix
C0019903molecular_functionprotein phosphatase binding
C0021766biological_processhippocampus development
C0030027cellular_componentlamellipodium
C0030036biological_processactin cytoskeleton organization
C0030042biological_processactin filament depolymerization
C0030043biological_processactin filament fragmentation
C0030175cellular_componentfilopodium
C0030307biological_processpositive regulation of cell growth
C0030424cellular_componentaxon
C0030426cellular_componentgrowth cone
C0030835biological_processnegative regulation of actin filament depolymerization
C0030836biological_processpositive regulation of actin filament depolymerization
C0030864cellular_componentcortical actin cytoskeleton
C0031252cellular_componentcell leading edge
C0031258cellular_componentlamellipodium membrane
C0031915biological_processpositive regulation of synaptic plasticity
C0031966cellular_componentmitochondrial membrane
C0031982cellular_componentvesicle
C0032232biological_processnegative regulation of actin filament bundle assembly
C0032587cellular_componentruffle membrane
C0040019biological_processpositive regulation of embryonic development
C0043025cellular_componentneuronal cell body
C0043066biological_processnegative regulation of apoptotic process
C0043197cellular_componentdendritic spine
C0044794biological_processhost-mediated activation of viral process
C0045862biological_processpositive regulation of proteolysis
C0050804biological_processmodulation of chemical synaptic transmission
C0051014biological_processactin filament severing
C0051015molecular_functionactin filament binding
C0051293biological_processestablishment of spindle localization
C0051511biological_processnegative regulation of unidimensional cell growth
C0051894biological_processpositive regulation of focal adhesion assembly
C0060999biological_processpositive regulation of dendritic spine development
C0061001biological_processregulation of dendritic spine morphogenesis
C0070062cellular_componentextracellular exosome
C0070301biological_processcellular response to hydrogen peroxide
C0071347biological_processcellular response to interleukin-1
C0071354biological_processcellular response to interleukin-6
C0071356biological_processcellular response to tumor necrosis factor
C0071362biological_processcellular response to ether
C0071364biological_processcellular response to epidermal growth factor stimulus
C0090732cellular_componentcofilin-actin rod
C0097060cellular_componentsynaptic membrane
C0098885biological_processmodification of postsynaptic actin cytoskeleton
C0098978cellular_componentglutamatergic synapse
C0099092cellular_componentpostsynaptic density, intracellular component
C1902936molecular_functionphosphatidylinositol bisphosphate binding
C1902951biological_processnegative regulation of dendritic spine maintenance
C1905873biological_processpositive regulation of protein localization to cell leading edge
C1905875biological_processnegative regulation of postsynaptic density organization
C1990314biological_processcellular response to insulin-like growth factor stimulus
C2000146biological_processnegative regulation of cell motility
C2000147biological_processpositive regulation of cell motility
C2000784biological_processpositive regulation of establishment of cell polarity regulating cell shape
C2000814biological_processpositive regulation of barbed-end actin filament capping
L0004672molecular_functionprotein kinase activity
L0005524molecular_functionATP binding
L0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue AGS L 701
ChainResidue
CCYS3
LASN465
LLEU467
LASP478
LLEU345
LVAL366
LLYS368
LGLU414
LILE416
LTHR420
LASP460
LHIS464
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGCFGQAIkVthretgev..........MVMK
ChainResidueDetails
LLEU345-LYS368
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by ROCK1 and PAK1","evidences":[{"source":"PubMed","id":"10559936","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10652353","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15660133","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23633677","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues149
DetailsDomain: {"description":"ADF-H","evidences":[{"source":"PROSITE-ProRule","id":"PRU00599","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsMotif: {"description":"Nuclear localization signal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"30550596","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2005","submissionDatabase":"UniProtKB","authors":["Quadroni M.","Bienvenut W.V."]}},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by NRK","evidences":[{"source":"PubMed","id":"12837278","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30550596","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P18760","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"30550596","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"30550596","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"30550596","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"30550596","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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