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1WUA

The structure of Aplyronine A-actin complex

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
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 1360
ChainResidue
AATP1380
AHOH1508
AHOH1509
AHOH1510
AHOH1511

site_idAC2
Number of Residues30
DetailsBINDING SITE FOR RESIDUE ATP A 1380
ChainResidue
ALYS18
AGLY156
AASP157
AGLY158
AVAL159
AGLY182
AARG210
ALYS213
AGLU214
AGLY301
AGLY302
ATHR303
AMET305
ATYR306
ACA1360
AHOH1403
AHOH1411
AHOH1423
AHOH1437
AHOH1449
AHOH1486
AHOH1508
AHOH1509
AHOH1510
AHOH1511
AHOH1823
AGLY13
ASER14
AGLY15
ALEU16

site_idAC3
Number of Residues29
DetailsBINDING SITE FOR RESIDUE AP8 A 1400
ChainResidue
ATYR69
AHIC73
ATYR133
ATYR143
AALA144
ASER145
AGLY146
AARG147
AGLY168
ATYR169
AARG183
AGLU334
ALEU349
ATHR351
APHE352
AMET355
AHOH1409
AHOH1415
AHOH1439
AHOH1443
AHOH1538
AHOH1571
AHOH1590
AHOH1639
AHOH1704
AHOH1775
AHOH1777
AHOH1816
AHOH1906

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 Residues1
DetailsMOD_RES: N-acetylaspartate; in Actin, alpha skeletal muscle => ECO:0000269|PubMed:1150665
ChainResidueDetails
AASP1

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134
ChainResidueDetails
AMET44
AMET47

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-malonyllysine => ECO:0000250
ChainResidueDetails
ALYS61

site_idSWS_FT_FI4
Number of Residues1
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

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133
ChainResidueDetails
ALYS84

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096
ChainResidueDetails
AARG177

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PDB entries from 2024-07-17

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