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

4PKG

Complex of ATP-actin With the N-terminal Actin-Binding Domain of Tropomodulin

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
G0005523molecular_functiontropomyosin binding
G0051015molecular_functionactin filament binding
G0051694biological_processpointed-end actin filament capping
Functional Information from PDB Data
site_idAC1
Number of Residues28
Detailsbinding site for residue ATP A 401
ChainResidue
AGLY13
AGLY182
AARG210
ALYS213
AGLU214
AGLY301
AGLY302
ATHR303
AMET305
ATYR306
ALYS336
ASER14
ACA402
AHOH555
AHOH556
AHOH557
AHOH561
AHOH571
AHOH579
AHOH731
AHOH736
AGLY15
ALEU16
ALYS18
AGLY156
AASP157
AGLY158
AVAL159

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 402
ChainResidue
AATP401
AHOH556
AHOH557
AHOH719
AHOH720
AHOH736

site_idAC3
Number of Residues6
Detailsbinding site for residue CA A 403
ChainResidue
AGLU167
AHOH699
GASP136
GGLY141
GALA143
GHOH1422

site_idAC4
Number of Residues6
Detailsbinding site for residue CA G 1201
ChainResidue
GGLY92
GASP93
GGLU124
GVAL172
GHOH1348
GHOH1360

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 Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:19666512, ECO:0007744|PDB:3FFK
ChainResidueDetails
GTHR132
GVAL133
GGLY164
GPHE176

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by SRC; in vitro => ECO:0000269|PubMed:10210201
ChainResidueDetails
GGLY126

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134
ChainResidueDetails
AMET44
AMET47

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-malonyllysine => ECO:0000250
ChainResidueDetails
ALYS61

site_idSWS_FT_FI5
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_FI6
Number of Residues1
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133
ChainResidueDetails
ALYS84

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096
ChainResidueDetails
AARG177

227344

PDB entries from 2024-11-13

PDB statisticsPDBj update infoContact PDBjnumon