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6Q9R

Crystal structure of the pathological N184K variant of calcium-free human gelsolin

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
A2001269biological_processpositive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway
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
B2001269biological_processpositive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue CL A 801
ChainResidue
AGLU126
AARG172
AHOH959

site_idAC2
Number of Residues1
Detailsbinding site for residue CL A 802
ChainResidue
AGLN409

site_idAC3
Number of Residues2
Detailsbinding site for residue CL A 803
ChainResidue
AGLU31
BLYS34

site_idAC4
Number of Residues3
Detailsbinding site for residue CL A 804
ChainResidue
ATYR453
AARG458
AHOH985

site_idAC5
Number of Residues1
Detailsbinding site for residue CL A 806
ChainResidue
ALYS503

site_idAC6
Number of Residues4
Detailsbinding site for residue GOL A 807
ChainResidue
AGLN540
AARG542
AASN562
AARG629

site_idAC7
Number of Residues3
Detailsbinding site for residue GOL A 808
ChainResidue
AASN196
AHOH935
BLYS150

site_idAC8
Number of Residues5
Detailsbinding site for residue GOL A 809
ChainResidue
AGLN364
AHIS638
APRO639
AARG641
AASP675

site_idAC9
Number of Residues6
Detailsbinding site for residue GOL A 810
ChainResidue
ALYS503
ATRP677
AASP678
AARG711
AASP712
ATHR715

site_idAD1
Number of Residues5
Detailsbinding site for residue GOL A 811
ChainResidue
AGLN296
ALEU299
AGLU355
AGLU358
ATRP369

site_idAD2
Number of Residues5
Detailsbinding site for residue GOL A 812
ChainResidue
ALYS272
AHIS309
AGLY310
ALYS311
ATYR344

site_idAD3
Number of Residues6
Detailsbinding site for residue GOL A 813
ChainResidue
AALA408
AGLN409
AGLY411
ATHR676
AASP678
ATRP732

site_idAD4
Number of Residues2
Detailsbinding site for residue GOL A 814
ChainResidue
AGLN496
ALYS693

site_idAD5
Number of Residues5
Detailsbinding site for residue SO4 A 815
ChainResidue
ATHR129
APRO360
ATYR382
ASER384
AARG641

site_idAD6
Number of Residues4
Detailsbinding site for residue SO4 A 816
ChainResidue
AARG207
AARG210
BARG207
BARG210

site_idAD7
Number of Residues2
Detailsbinding site for residue CL B 801
ChainResidue
BTYR87
BARG120

site_idAD8
Number of Residues2
Detailsbinding site for residue CL B 802
ChainResidue
BARG542
BARG629

site_idAD9
Number of Residues5
Detailsbinding site for residue GOL B 804
ChainResidue
BGLY723
BGLU725
BTRP736
BASP738
BTRP741

site_idAE1
Number of Residues10
Detailsbinding site for residue GOL B 805
ChainResidue
BASP413
BILE462
BTYR464
BPRO505
BGLN679
BPHE681
BTHR718
BPRO726
BSER728
BHOH936

site_idAE2
Number of Residues5
Detailsbinding site for residue GOL B 806
ChainResidue
BLYS503
BTRP677
BARG711
BASP712
BTHR715

site_idAE3
Number of Residues6
Detailsbinding site for residue GOL B 807
ChainResidue
BTHR129
BTHR359
BPRO360
BLEU361
BSER384
BARG641

site_idAE4
Number of Residues6
Detailsbinding site for residue GOL B 808
ChainResidue
BGLN364
BHIS638
BPRO639
BARG641
BASP675
BTRP677

site_idAE5
Number of Residues6
Detailsbinding site for residue GOL B 809
ChainResidue
BALA408
BGLN409
BLYS634
BTHR676
BASP678
BHOH946

site_idAE6
Number of Residues3
Detailsbinding site for residue GOL B 810
ChainResidue
BLYS721
BLYS686
BLYS693

site_idAE7
Number of Residues4
Detailsbinding site for residue GOL B 811
ChainResidue
BTYR59
BTYR133
BPHE134
BLYS135

site_idAE8
Number of Residues4
Detailsbinding site for residue GOL B 812
ChainResidue
BGLN722
BGLY723
BTRP741
BHOH911

site_idAE9
Number of Residues5
Detailsbinding site for residue TRS B 813
ChainResidue
ATHR375
AASP376
BTHR417
BGLY418
BLYS420

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
BASP187
BGLU209
BASP259
BGLU302
BASP303
BGLU327
AGLU97
AASP109
AGLY114
AALA116
AVAL145
AGLY186
AASP187

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

223166

PDB entries from 2024-07-31

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