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6JEH

Crystal structure of calcium free human gelsolin amyloid mutant D187Y

Functional Information from GO Data
ChainGOidnamespacecontents
A0002102cellular_componentpodosome
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
A0016192biological_processvesicle-mediated transport
A0016528cellular_componentsarcoplasm
A0022617biological_processextracellular matrix disassembly
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
A0042989biological_processsequestering of actin monomers
A0045159molecular_functionmyosin II binding
A0045335cellular_componentphagocytic vesicle
A0046597biological_processnegative regulation of viral entry into host cell
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
A0071346biological_processcellular response to type II interferon
A0071801biological_processregulation of podosome assembly
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
A2001056biological_processpositive regulation of cysteine-type endopeptidase activity
B0002102cellular_componentpodosome
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
B0016192biological_processvesicle-mediated transport
B0016528cellular_componentsarcoplasm
B0022617biological_processextracellular matrix disassembly
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
B0042989biological_processsequestering of actin monomers
B0045159molecular_functionmyosin II binding
B0045335cellular_componentphagocytic vesicle
B0046597biological_processnegative regulation of viral entry into host cell
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
B0071346biological_processcellular response to type II interferon
B0071801biological_processregulation of podosome assembly
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
B2001056biological_processpositive regulation of cysteine-type endopeptidase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues28
DetailsBINDING: BINDING => ECO:0000269|PubMed:19666512, ECO:0007744|PDB:3FFK
ChainResidueDetails
AGLY65
AGLU209
AASP259
AGLU302
AASP303
AGLU327
BGLY65
BASP66
BGLU97
BASP109
BGLY114
AASP66
BALA116
BVAL145
BGLY186
BTYR187
BGLU209
BASP259
BGLU302
BASP303
BGLU327
AGLU97
AASP109
AGLY114
AALA116
AVAL145
AGLY186
ATYR187

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS135
AARG161
BLYS135
BARG161

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12460571, ECO:0000269|PubMed:16466744, ECO:0007744|PDB:1H1V, ECO:0007744|PDB:2FH2, ECO:0007744|PDB:2FH3
ChainResidueDetails
AGLY444
AGLU587
BGLY444
BGLU587

site_idSWS_FT_FI4
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:12460571, ECO:0000269|PubMed:16466744, ECO:0007744|PDB:1H1V, ECO:0007744|PDB:2FH1, ECO:0007744|PDB:2FH2, ECO:0007744|PDB:2FH3
ChainResidueDetails
AASP445
BTHR524
BASN564
BASP565
BASP669
BGLU692
AGLU475
ATHR524
AASN564
AASP565
AASP669
AGLU692
BASP445
BGLU475

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:12460571, ECO:0007744|PDB:1H1V
ChainResidueDetails
AASP487
AGLY492
APRO494
BASP487
BGLY492
BPRO494

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12460571, ECO:0000269|PubMed:16466744, ECO:0007744|PDB:1H1V, ECO:0007744|PDB:2FH3
ChainResidueDetails
AASP670
BASP670

site_idSWS_FT_FI7
Number of Residues8
DetailsMOD_RES: Phosphotyrosine; by SRC; in vitro => ECO:0000269|PubMed:10210201
ChainResidueDetails
ATYR59
ATYR382
ATYR576
ATYR624
BTYR59
BTYR382
BTYR576
BTYR624

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by SRC => ECO:0000269|PubMed:10210201
ChainResidueDetails
ATYR438
BTYR438

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P13020
ChainResidueDetails
ALYS557
BLYS557

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR715
BTHR715

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PDB entries from 2024-11-06

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