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1YXQ

Crystal structure of actin in complex with swinholide A

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0001725cellular_componentstress fiber
A0003785molecular_functionactin monomer binding
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005523molecular_functiontropomyosin binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005865cellular_componentstriated muscle thin filament
A0005884cellular_componentactin filament
A0010628biological_processpositive regulation of gene expression
A0016787molecular_functionhydrolase activity
A0019904molecular_functionprotein domain specific binding
A0030027cellular_componentlamellipodium
A0030041biological_processactin filament polymerization
A0030175cellular_componentfilopodium
A0030240biological_processskeletal muscle thin filament assembly
A0031013molecular_functiontroponin I binding
A0031432molecular_functiontitin binding
A0031941cellular_componentfilamentous actin
A0032036molecular_functionmyosin heavy chain binding
A0032432cellular_componentactin filament bundle
A0042802molecular_functionidentical protein binding
A0044297cellular_componentcell body
A0048306molecular_functioncalcium-dependent protein binding
A0048741biological_processskeletal muscle fiber development
A0051017biological_processactin filament bundle assembly
A0090131biological_processmesenchyme migration
A0098723cellular_componentskeletal muscle myofibril
A0140660molecular_functioncytoskeletal motor activator activity
B0000287molecular_functionmagnesium ion binding
B0001725cellular_componentstress fiber
B0003785molecular_functionactin monomer binding
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005523molecular_functiontropomyosin binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005856cellular_componentcytoskeleton
B0005865cellular_componentstriated muscle thin filament
B0005884cellular_componentactin filament
B0010628biological_processpositive regulation of gene expression
B0016787molecular_functionhydrolase activity
B0019904molecular_functionprotein domain specific binding
B0030027cellular_componentlamellipodium
B0030041biological_processactin filament polymerization
B0030175cellular_componentfilopodium
B0030240biological_processskeletal muscle thin filament assembly
B0031013molecular_functiontroponin I binding
B0031432molecular_functiontitin binding
B0031941cellular_componentfilamentous actin
B0032036molecular_functionmyosin heavy chain binding
B0032432cellular_componentactin filament bundle
B0042802molecular_functionidentical protein binding
B0044297cellular_componentcell body
B0048306molecular_functioncalcium-dependent protein binding
B0048741biological_processskeletal muscle fiber development
B0051017biological_processactin filament bundle assembly
B0090131biological_processmesenchyme migration
B0098723cellular_componentskeletal muscle myofibril
B0140660molecular_functioncytoskeletal motor activator activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1390
ChainResidue
AATP1380
AHOH9002
AHOH9003
AHOH9004
AHOH9005

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 2390
ChainResidue
BHOH9006
BATP2380
BHOH9003
BHOH9004
BHOH9005

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 5001
ChainResidue
AGLU205
AHOH9006
AHOH9007
AHOH9008
AHOH9009
AHOH9010

site_idAC4
Number of Residues29
DetailsBINDING SITE FOR RESIDUE ATP A 1380
ChainResidue
AGLY13
ASER14
AGLY15
ALEU16
ALYS18
AGLY156
AASP157
AGLY182
AARG183
AARG210
ALYS213
AGLU214
AGLY301
AGLY302
ATHR303
AMET305
ATYR306
ALYS336
AMG1390
AHOH9003
AHOH9004
AHOH9005
AHOH9064
AHOH9083
AHOH9089
AHOH9098
AHOH9169
AHOH9175
AHOH9190

site_idAC5
Number of Residues23
DetailsBINDING SITE FOR RESIDUE ATP B 2380
ChainResidue
BGLY13
BSER14
BGLY15
BLEU16
BLYS18
BGLY156
BASP157
BGLY158
BVAL159
BGLY182
BARG210
BLYS213
BGLU214
BGLY301
BGLY302
BTHR303
BMET305
BTYR306
BMG2390
BHOH9003
BHOH9004
BHOH9005
BHOH9006

site_idAC6
Number of Residues33
DetailsBINDING SITE FOR RESIDUE SWI B 600
ChainResidue
BHOH9033
BHOH9036
AASP24
AASP25
ATYR143
AALA144
ASER145
AGLY146
ATYR169
ASER344
AILE345
ASER348
ALEU349
ATHR351
AMET355
AHOH9224
BGLY23
BASP24
BTYR133
BTYR143
BALA144
BSER145
BGLY146
BARG147
BILE341
BSER344
BSER348
BLEU349
BTHR351
BMET355
BHOH9011
BHOH9013
BHOH9027

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 9001
ChainResidue
AALA144
ASER145
APRO332
AGLU334
AILE341
AHOH9176
AHOH9222

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 9002
ChainResidue
BALA144
BPRO332

Functional Information from PROSITE/UniProt
site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. YVGDEAQs.KRG
ChainResidueDetails
ATYR53-GLY63

site_idPS00432
Number of Residues9
DetailsACTINS_2 Actins signature 2. WITKqEYDE
ChainResidueDetails
ATRP356-GLU364

site_idPS01132
Number of Residues13
DetailsACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR
ChainResidueDetails
ALEU104-ARG116

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N-acetylaspartate; in Actin, alpha skeletal muscle => ECO:0000269|PubMed:1150665
ChainResidueDetails
AASP1
BASP1

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134
ChainResidueDetails
AMET44
AMET47
BMET44
BMET47

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-malonyllysine => ECO:0000250
ChainResidueDetails
ALYS61
BLYS61

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Tele-methylhistidine => ECO:0000269|PubMed:1150665, ECO:0000269|PubMed:16905096, ECO:0000269|PubMed:213279, ECO:0000269|PubMed:2395459, ECO:0000269|PubMed:499690, ECO:0007744|PDB:1ATN, ECO:0007744|PDB:1NWK
ChainResidueDetails
AHIC73
BHIC73

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133
ChainResidueDetails
ALYS84
BLYS84

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096
ChainResidueDetails
AARG177
BARG177

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PDB entries from 2024-07-17

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