Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1RDW

Actin Crystal Dynamics: Structural Implications for F-actin Nucleation, Polymerization and Branching Mediated by the Anti-parallel Dimer

Functional Information from GO Data
ChainGOidnamespacecontents
X0000166molecular_functionnucleotide binding
X0000287molecular_functionmagnesium ion binding
X0001725cellular_componentstress fiber
X0003785molecular_functionactin monomer binding
X0005509molecular_functioncalcium ion binding
X0005515molecular_functionprotein binding
X0005523molecular_functiontropomyosin binding
X0005524molecular_functionATP binding
X0005737cellular_componentcytoplasm
X0005856cellular_componentcytoskeleton
X0005865cellular_componentstriated muscle thin filament
X0005884cellular_componentactin filament
X0010628biological_processpositive regulation of gene expression
X0016787molecular_functionhydrolase activity
X0019904molecular_functionprotein domain specific binding
X0030027cellular_componentlamellipodium
X0030041biological_processactin filament polymerization
X0030175cellular_componentfilopodium
X0030240biological_processskeletal muscle thin filament assembly
X0031013molecular_functiontroponin I binding
X0031432molecular_functiontitin binding
X0031941cellular_componentfilamentous actin
X0032036molecular_functionmyosin heavy chain binding
X0032432cellular_componentactin filament bundle
X0042802molecular_functionidentical protein binding
X0044297cellular_componentcell body
X0048306molecular_functioncalcium-dependent protein binding
X0048741biological_processskeletal muscle fiber development
X0051017biological_processactin filament bundle assembly
X0090131biological_processmesenchyme migration
X0098723cellular_componentskeletal muscle myofibril
X0140660molecular_functioncytoskeletal motor activator activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG X 392
ChainResidue
XATP390
XHOH423
XHOH424
XHOH425
XHOH426
XHOH472

site_idAC2
Number of Residues28
DetailsBINDING SITE FOR RESIDUE ATP X 390
ChainResidue
XLEU16
XLYS18
XGLY156
XASP157
XGLY158
XVAL159
XGLY182
XARG210
XLYS213
XGLU214
XGLY301
XGLY302
XTHR303
XMET305
XTYR306
XLAR391
XMG392
XHOH401
XHOH404
XHOH419
XHOH425
XHOH426
XHOH440
XHOH460
XHOH472
XGLY13
XSER14
XGLY15

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE LAR X 391
ChainResidue
XGLY15
XLEU16
XGLN59
XTYR69
XASP157
XARG183
XTHR186
XARG206
XGLU207
XARG210
XLYS213
XATP390
XHOH474

Functional Information from PROSITE/UniProt
site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. YVGDEAQs.KRG
ChainResidueDetails
XTYR53-GLY63

site_idPS00432
Number of Residues9
DetailsACTINS_2 Actins signature 2. WITKqEYDE
ChainResidueDetails
XTRP356-GLU364

site_idPS01132
Number of Residues13
DetailsACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR
ChainResidueDetails
XLEU104-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
XASP1

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134
ChainResidueDetails
XMET44
XMET47

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-malonyllysine => ECO:0000250
ChainResidueDetails
XLYS61

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
XHIS73

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133
ChainResidueDetails
XLYS84

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096
ChainResidueDetails
XARG177

237423

PDB entries from 2025-06-11

PDB statisticsPDBj update infoContact PDBjnumon