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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6QBF

Crystal structure of the pathological D187N variant of calcium-free human gelsolin.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003779molecular_functionactin binding
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0005925cellular_componentfocal adhesion
A0006911biological_processphagocytosis, engulfment
A0007015biological_processactin filament organization
A0007417biological_processcentral nervous system development
A0008154biological_processactin polymerization or depolymerization
A0010628biological_processpositive regulation of gene expression
A0014891biological_processstriated muscle atrophy
A0015629cellular_componentactin cytoskeleton
A0016528cellular_componentsarcoplasm
A0030027cellular_componentlamellipodium
A0030030biological_processcell projection organization
A0030031biological_processcell projection assembly
A0030036biological_processactin cytoskeleton organization
A0030041biological_processactin filament polymerization
A0030042biological_processactin filament depolymerization
A0030478cellular_componentactin cap
A0030864cellular_componentcortical actin cytoskeleton
A0031648biological_processprotein destabilization
A0034774cellular_componentsecretory granule lumen
A0035994biological_processresponse to muscle stretch
A0036313molecular_functionphosphatidylinositol 3-kinase catalytic subunit binding
A0043065biological_processpositive regulation of apoptotic process
A0045159molecular_functionmyosin II binding
A0045335cellular_componentphagocytic vesicle
A0046597biological_processhost-mediated suppression of symbiont invasion
A0046872molecular_functionmetal ion binding
A0051014biological_processactin filament severing
A0051015molecular_functionactin filament binding
A0051016biological_processbarbed-end actin filament capping
A0051127biological_processpositive regulation of actin nucleation
A0051693biological_processactin filament capping
A0055119biological_processrelaxation of cardiac muscle
A0060271biological_processcilium assembly
A0070062cellular_componentextracellular exosome
A0072562cellular_componentblood microparticle
A0086003biological_processcardiac muscle cell contraction
A0097017biological_processrenal protein absorption
A0097284biological_processhepatocyte apoptotic process
A1902174biological_processpositive regulation of keratinocyte apoptotic process
A1903903biological_processregulation of establishment of T cell polarity
A1903906biological_processregulation of plasma membrane raft polarization
A1903909biological_processregulation of receptor clustering
A1903923biological_processpositive regulation of protein processing in phagocytic vesicle
A1904813cellular_componentficolin-1-rich granule lumen
A1990000biological_processamyloid fibril formation
B0003779molecular_functionactin binding
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005886cellular_componentplasma membrane
B0005925cellular_componentfocal adhesion
B0006911biological_processphagocytosis, engulfment
B0007015biological_processactin filament organization
B0007417biological_processcentral nervous system development
B0008154biological_processactin polymerization or depolymerization
B0010628biological_processpositive regulation of gene expression
B0014891biological_processstriated muscle atrophy
B0015629cellular_componentactin cytoskeleton
B0016528cellular_componentsarcoplasm
B0030027cellular_componentlamellipodium
B0030030biological_processcell projection organization
B0030031biological_processcell projection assembly
B0030036biological_processactin cytoskeleton organization
B0030041biological_processactin filament polymerization
B0030042biological_processactin filament depolymerization
B0030478cellular_componentactin cap
B0030864cellular_componentcortical actin cytoskeleton
B0031648biological_processprotein destabilization
B0034774cellular_componentsecretory granule lumen
B0035994biological_processresponse to muscle stretch
B0036313molecular_functionphosphatidylinositol 3-kinase catalytic subunit binding
B0043065biological_processpositive regulation of apoptotic process
B0045159molecular_functionmyosin II binding
B0045335cellular_componentphagocytic vesicle
B0046597biological_processhost-mediated suppression of symbiont invasion
B0046872molecular_functionmetal ion binding
B0051014biological_processactin filament severing
B0051015molecular_functionactin filament binding
B0051016biological_processbarbed-end actin filament capping
B0051127biological_processpositive regulation of actin nucleation
B0051693biological_processactin filament capping
B0055119biological_processrelaxation of cardiac muscle
B0060271biological_processcilium assembly
B0070062cellular_componentextracellular exosome
B0072562cellular_componentblood microparticle
B0086003biological_processcardiac muscle cell contraction
B0097017biological_processrenal protein absorption
B0097284biological_processhepatocyte apoptotic process
B1902174biological_processpositive regulation of keratinocyte apoptotic process
B1903903biological_processregulation of establishment of T cell polarity
B1903906biological_processregulation of plasma membrane raft polarization
B1903909biological_processregulation of receptor clustering
B1903923biological_processpositive regulation of protein processing in phagocytic vesicle
B1904813cellular_componentficolin-1-rich granule lumen
B1990000biological_processamyloid fibril formation
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue SO4 A 801
ChainResidue
AGLN164
AASN184
ATHR257
site_idAC2
Number of Residues7
Detailsbinding site for residue GOL A 802
ChainResidue
ATRP732
AALA408
AGLN409
ALYS634
AMET635
ATHR676
AASP678
site_idAC3
Number of Residues6
Detailsbinding site for residue SO4 B 801
ChainResidue
BTHR129
BLEU361
BTYR382
BSER384
BHIS386
BARG641
site_idAC4
Number of Residues3
Detailsbinding site for residue NA B 802
ChainResidue
BGLU725
BTRP736
BASP738
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues164
DetailsRepeat: {"description":"Gelsolin-like 1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues144
DetailsRepeat: {"description":"Gelsolin-like 2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues144
DetailsRepeat: {"description":"Gelsolin-like 3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues162
DetailsRepeat: {"description":"Gelsolin-like 4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues66
DetailsRepeat: {"description":"Gelsolin-like 5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues150
DetailsRepeat: {"description":"Gelsolin-like 6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues6
DetailsRegion: {"description":"Actin-actin interfilament contact point"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues76
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues30
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues26
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19666512","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FFK","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues30
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12460571","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16466744","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1H1V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FH2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FH3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12460571","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16466744","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1H1V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FH1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FH2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FH3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12460571","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1H1V","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12460571","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16466744","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1H1V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FH3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues8
DetailsModified residue: {"description":"Phosphotyrosine; by SRC; in vitro","evidences":[{"source":"PubMed","id":"10210201","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by SRC","evidences":[{"source":"PubMed","id":"10210201","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P13020","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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