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5L6W

Structure Of the LIMK1-ATPgammaS-CFL1 Complex

Functional Information from GO Data
ChainGOidnamespacecontents
C0000281biological_processmitotic cytokinesis
C0003779molecular_functionactin binding
C0005515molecular_functionprotein binding
C0005615cellular_componentextracellular space
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005856cellular_componentcytoskeleton
C0005886cellular_componentplasma membrane
C0005925cellular_componentfocal adhesion
C0007010biological_processcytoskeleton organization
C0007266biological_processRho protein signal transduction
C0009615biological_processresponse to virus
C0015629cellular_componentactin cytoskeleton
C0016020cellular_componentmembrane
C0016363cellular_componentnuclear matrix
C0022604biological_processregulation of cell morphogenesis
C0030027cellular_componentlamellipodium
C0030036biological_processactin cytoskeleton organization
C0030042biological_processactin filament depolymerization
C0030043biological_processactin filament fragmentation
C0030424cellular_componentaxon
C0030426cellular_componentgrowth cone
C0031258cellular_componentlamellipodium membrane
C0031982cellular_componentvesicle
C0032587cellular_componentruffle membrane
C0040019biological_processpositive regulation of embryonic development
C0042995cellular_componentcell projection
C0043066biological_processnegative regulation of apoptotic process
C0044794biological_processpositive regulation by host of viral process
C0051014biological_processactin filament severing
C0051015molecular_functionactin filament binding
C0051293biological_processestablishment of spindle localization
C0061001biological_processregulation of dendritic spine morphogenesis
C0070062cellular_componentextracellular exosome
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
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:30550596, ECO:0000269|Ref.9, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
ChainResidueDetails
CALA2

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine; by NRK => ECO:0000269|PubMed:12837278, ECO:0000269|PubMed:30550596, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
CCYS3
LLYS368

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P18760
ChainResidueDetails
CSER8

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
CLYS13
CLYS73
CLYS144

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231
ChainResidueDetails
CTHR25

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
CSER41

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:30550596
ChainResidueDetails
CTHR63

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332
ChainResidueDetails
CTYR68

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:30550596
ChainResidueDetails
CTYR82

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:30550596
ChainResidueDetails
CSER108

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
CTYR140

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:30550596, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
CSER156

site_idSWS_FT_FI13
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
CLYS132

227344

PDB entries from 2024-11-13

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