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2FGH

ATP bound gelsolin

Functional Information from GO Data
ChainGOidnamespacecontents
A0003779molecular_functionactin binding
A0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0007417biological_processcentral nervous system development
A0008154biological_processactin polymerization or depolymerization
A0015629cellular_componentactin cytoskeleton
A0030030biological_processcell projection organization
A0030031biological_processcell projection assembly
A0046872molecular_functionmetal ion binding
A0051014biological_processactin filament severing
A0051015molecular_functionactin filament binding
A0051016biological_processbarbed-end actin filament capping
A0051693biological_processactin filament capping
A0060271biological_processcilium assembly
B0003779molecular_functionactin binding
B0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005856cellular_componentcytoskeleton
B0007417biological_processcentral nervous system development
B0008154biological_processactin polymerization or depolymerization
B0015629cellular_componentactin cytoskeleton
B0030030biological_processcell projection organization
B0030031biological_processcell projection assembly
B0046872molecular_functionmetal ion binding
B0051014biological_processactin filament severing
B0051015molecular_functionactin filament binding
B0051016biological_processbarbed-end actin filament capping
B0051693biological_processactin filament capping
B0060271biological_processcilium assembly
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ATP A 5380
ChainResidue
AARG363
AHIS638
AASN368
ATRP369
AARG370
AASP371
ALYS503
AARG542
AARG629
ALEU630

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ATP B 9380
ChainResidue
BARG363
BASN368
BTRP369
BARG370
BASP371
BLYS503
BARG542
BARG629
BLEU630
BHIS638
BHOH9400

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBINDING: BINDING => ECO:0000269|PubMed:15215896, ECO:0007744|PDB:1RGI
ChainResidueDetails
AASP66
AARG328
BASP66
BALA67
BSER98
BASP110
BARG115
BVAL117
BALA146
BASP303
BCYS304
AALA67
BARG328
ASER98
AASP110
AARG115
AVAL117
AALA146
AASP303
ACYS304

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ASER136
ALEU162
BSER136
BLEU162

site_idSWS_FT_FI3
Number of Residues34
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P06396
ChainResidueDetails
AASP187
AVAL495
ASER525
AASP565
AALA566
ALYS588
AASP670
AVAL671
ALYS693
BASP187
BCYS188
ACYS188
BARG210
BTHR260
BASP445
BSER446
BVAL476
BGLU488
BTHR493
BVAL495
BSER525
BASP565
AARG210
BALA566
BLYS588
BASP670
BVAL671
BLYS693
ATHR260
AASP445
ASER446
AVAL476
AGLU488
ATHR493

site_idSWS_FT_FI4
Number of Residues10
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P06396
ChainResidueDetails
AGLY60
BARG625
ALEU383
AGLY439
ALEU577
AARG625
BGLY60
BLEU383
BGLY439
BLEU577

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P13020
ChainResidueDetails
AALA558
BALA558

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P06396
ChainResidueDetails
APRO716
BPRO716

218853

PDB entries from 2024-04-24

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