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

5HVK

Crystal structure of LIMK1 mutant D460N in complex with full-length cofilin-1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0000281biological_processmitotic cytokinesis
B0003779molecular_functionactin binding
B0005515molecular_functionprotein binding
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005886cellular_componentplasma membrane
B0005925cellular_componentfocal adhesion
B0007010biological_processcytoskeleton organization
B0007266biological_processRho protein signal transduction
B0009615biological_processresponse to virus
B0015629cellular_componentactin cytoskeleton
B0016020cellular_componentmembrane
B0016363cellular_componentnuclear matrix
B0022604biological_processregulation of cell morphogenesis
B0030027cellular_componentlamellipodium
B0030036biological_processactin cytoskeleton organization
B0030042biological_processactin filament depolymerization
B0030043biological_processactin filament fragmentation
B0030424cellular_componentaxon
B0030426cellular_componentgrowth cone
B0031258cellular_componentlamellipodium membrane
B0031982cellular_componentvesicle
B0032587cellular_componentruffle membrane
B0040019biological_processpositive regulation of embryonic development
B0042995cellular_componentcell projection
B0043066biological_processnegative regulation of apoptotic process
B0044794biological_processpositive regulation by host of viral process
B0051014biological_processactin filament severing
B0051015molecular_functionactin filament binding
B0051293biological_processestablishment of spindle localization
B0061001biological_processregulation of dendritic spine morphogenesis
B0070062cellular_componentextracellular exosome
C0004672molecular_functionprotein kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
D0000281biological_processmitotic cytokinesis
D0003779molecular_functionactin binding
D0005515molecular_functionprotein binding
D0005615cellular_componentextracellular space
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005856cellular_componentcytoskeleton
D0005886cellular_componentplasma membrane
D0005925cellular_componentfocal adhesion
D0007010biological_processcytoskeleton organization
D0007266biological_processRho protein signal transduction
D0009615biological_processresponse to virus
D0015629cellular_componentactin cytoskeleton
D0016020cellular_componentmembrane
D0016363cellular_componentnuclear matrix
D0022604biological_processregulation of cell morphogenesis
D0030027cellular_componentlamellipodium
D0030036biological_processactin cytoskeleton organization
D0030042biological_processactin filament depolymerization
D0030043biological_processactin filament fragmentation
D0030424cellular_componentaxon
D0030426cellular_componentgrowth cone
D0031258cellular_componentlamellipodium membrane
D0031982cellular_componentvesicle
D0032587cellular_componentruffle membrane
D0040019biological_processpositive regulation of embryonic development
D0042995cellular_componentcell projection
D0043066biological_processnegative regulation of apoptotic process
D0044794biological_processpositive regulation by host of viral process
D0051014biological_processactin filament severing
D0051015molecular_functionactin filament binding
D0051293biological_processestablishment of spindle localization
D0061001biological_processregulation of dendritic spine morphogenesis
D0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue ANP A 1001
ChainResidue
ALEU345
ATHR420
AASN465
ALEU467
AASP478
AMG1002
BSEP3
ACYS349
AGLY351
AVAL366
ALYS368
ALEU397
ATHR413
AGLU414
AILE416

site_idAC2
Number of Residues3
Detailsbinding site for residue MG A 1002
ChainResidue
AHIS464
AASN465
AANP1001

site_idAC3
Number of Residues14
Detailsbinding site for residue ANP C 701
ChainResidue
CLEU345
CGLY351
CVAL366
CLYS368
CLEU397
CTHR413
CGLU414
CILE416
CTHR420
CLEU467
CASP478
CMG702
DALA2
DSER3

site_idAC4
Number of Residues3
Detailsbinding site for residue MG C 702
ChainResidue
CHIS464
CASN465
CANP701

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGCFGQAIkVthretgev..........MVMK
ChainResidueDetails
ALEU345-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
DALA2
CASN460

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
DSER3
ALYS368
CLEU345
CLYS368

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P18760
ChainResidueDetails
DSER8
CSER337

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
DLYS13
DLYS73
DLYS144

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231
ChainResidueDetails
DTHR25

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
DSER41

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:30550596
ChainResidueDetails
DTHR63

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332
ChainResidueDetails
DTYR68

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:30550596
ChainResidueDetails
DTYR82

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:30550596
ChainResidueDetails
DSER108

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
DTYR140

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
DSER156

site_idSWS_FT_FI13
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
DLYS132

222036

PDB entries from 2024-07-03

PDB statisticsPDBj update infoContact PDBjnumon