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5ZZB

LokiProfilin2/Rabbit Actin Complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0003779molecular_functionactin binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
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
C0003779molecular_functionactin binding
C0005737cellular_componentcytoplasm
C0005856cellular_componentcytoskeleton
D0000287molecular_functionmagnesium ion binding
D0001725cellular_componentstress fiber
D0003785molecular_functionactin monomer binding
D0005509molecular_functioncalcium ion binding
D0005515molecular_functionprotein binding
D0005523molecular_functiontropomyosin binding
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005856cellular_componentcytoskeleton
D0005865cellular_componentstriated muscle thin filament
D0005884cellular_componentactin filament
D0010628biological_processpositive regulation of gene expression
D0016787molecular_functionhydrolase activity
D0019904molecular_functionprotein domain specific binding
D0030027cellular_componentlamellipodium
D0030041biological_processactin filament polymerization
D0030175cellular_componentfilopodium
D0030240biological_processskeletal muscle thin filament assembly
D0031013molecular_functiontroponin I binding
D0031432molecular_functiontitin binding
D0031941cellular_componentfilamentous actin
D0032036molecular_functionmyosin heavy chain binding
D0032432cellular_componentactin filament bundle
D0042802molecular_functionidentical protein binding
D0044297cellular_componentcell body
D0048306molecular_functioncalcium-dependent protein binding
D0048741biological_processskeletal muscle fiber development
D0051017biological_processactin filament bundle assembly
D0090131biological_processmesenchyme migration
D0098723cellular_componentskeletal muscle myofibril
D0140660molecular_functioncytoskeletal motor activator activity
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue LAB B 401
ChainResidue
BGLY15
BGLU207
BARG210
BHOH580
BLEU16
BGLN59
BARG62
BTYR69
BASP157
BARG183
BTHR186
BARG206

site_idAC2
Number of Residues24
Detailsbinding site for residue ATP B 402
ChainResidue
BGLY13
BSER14
BGLY15
BLEU16
BLYS18
BGLY156
BASP157
BGLY158
BVAL159
BGLY182
BARG210
BLYS213
BGLU214
BGLY301
BGLY302
BTHR303
BMET305
BTYR306
BLYS336
BCA403
BHOH530
BHOH583
BHOH595
BHOH610

site_idAC3
Number of Residues6
Detailsbinding site for residue CA B 403
ChainResidue
BATP402
BHOH517
BHOH530
BHOH532
BHOH587
BHOH595

site_idAC4
Number of Residues12
Detailsbinding site for residue LAB D 401
ChainResidue
DGLY15
DLEU16
DGLN59
DTYR69
DASP157
DARG183
DTHR186
DARG206
DGLU207
DARG210
DLYS213
DHOH620

site_idAC5
Number of Residues26
Detailsbinding site for residue ATP D 402
ChainResidue
DGLY13
DSER14
DGLY15
DLEU16
DLYS18
DGLY156
DASP157
DGLY158
DVAL159
DGLY182
DARG210
DLYS213
DGLU214
DGLY301
DGLY302
DTHR303
DMET305
DTYR306
DLYS336
DCA403
DHOH523
DHOH539
DHOH563
DHOH614
DHOH625
DHOH626

site_idAC6
Number of Residues6
Detailsbinding site for residue CA D 403
ChainResidue
DATP402
DHOH523
DHOH541
DHOH543
DHOH597
DHOH625

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 Residues4
DetailsMOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134
ChainResidueDetails
BMET44
BMET47
DMET44
DMET47

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-malonyllysine => ECO:0000250
ChainResidueDetails
BLYS61
DLYS61

site_idSWS_FT_FI3
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
BHIS73
DHIS73

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133
ChainResidueDetails
BLYS84
DLYS84

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096
ChainResidueDetails
BARG177
DARG177

224201

PDB entries from 2024-08-28

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