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3BUZ

Crystal structure of ia-bTAD-actin complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005576cellular_componentextracellular region
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 Residues4
DetailsBINDING SITE FOR RESIDUE CA B 500
ChainResidue
BHOH926
BHOH930
BHOH931
BHOH936

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE TAD A 500
ChainResidue
AGLY298
AGLN300
AGLU301
ATYR333
APRO334
AASN335
ASER338
APHE349
AARG352
AGLU380
ATYR251
AASN255
AILE259
AARG295
AARG296

site_idAC3
Number of Residues23
DetailsBINDING SITE FOR RESIDUE ATP B 380
ChainResidue
BGLY13
BSER14
BGLY15
BLEU16
BLYS18
BGLY156
BASP157
BGLY158
BGLY182
BARG210
BLYS213
BGLU214
BGLY301
BGLY302
BTHR303
BMET305
BTYR306
BLYS336
BHOH906
BHOH925
BHOH926
BHOH929
BHOH930

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE LAR B 901
ChainResidue
BLEU16
BPRO32
BGLN59
BTYR69
BASP157
BARG183
BTHR186
BGLU207
BARG210

Functional Information from PROSITE/UniProt
site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. YVGDEAQs.KRG
ChainResidueDetails
BTYR53-GLY63

site_idPS00432
Number of Residues9
DetailsACTINS_2 Actins signature 2. WITKqEYDE
ChainResidueDetails
BTRP356-GLU364

site_idPS01132
Number of Residues13
DetailsACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR
ChainResidueDetails
BLEU104-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
BASP1

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134
ChainResidueDetails
BMET44
BMET47

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-malonyllysine => ECO:0000250
ChainResidueDetails
BLYS61

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
BHIS73

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133
ChainResidueDetails
BLYS84

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096
ChainResidueDetails
BARG177

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PDB entries from 2024-05-01

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