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2V51

Structure of MAL-RPEL1 complexed to actin

Functional Information from GO Data
ChainGOidnamespacecontents
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
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 Residues26
DetailsBINDING SITE FOR RESIDUE ATP B1372
ChainResidue
BGLY13
BGLY182
BARG210
BLYS213
BGLU214
BGLY301
BGLY302
BMET305
BTYR306
BLYS336
BCA1373
BSER14
BLAB1374
BHOH2038
BHOH2076
BHOH2093
BHOH2101
BHOH2102
BHOH2103
BGLY15
BLEU16
BLYS18
BGLY156
BASP157
BGLY158
BVAL159

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B1373
ChainResidue
BATP1372
BHOH2002
BHOH2003
BHOH2038
BHOH2102

site_idAC3
Number of Residues27
DetailsBINDING SITE FOR RESIDUE ATP D1372
ChainResidue
DGLY13
DSER14
DGLY15
DLEU16
DLYS18
DGLY156
DASP157
DGLY158
DVAL159
DGLY182
DARG210
DLYS213
DGLU214
DGLY301
DGLY302
DMET305
DTYR306
DLYS336
DCA1373
DLAB1374
DHOH2042
DHOH2043
DHOH2049
DHOH2080
DHOH2093
DHOH2095
DHOH2096

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA D1373
ChainResidue
DATP1372
DHOH2003
DHOH2004
DHOH2042
DHOH2049

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE LAB B1374
ChainResidue
BGLY15
BPRO32
BTYR69
BASP157
BTHR186
BARG206
BGLU207
BARG210
BLYS213
BATP1372

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PEG B1375
ChainResidue
BLYS238
BARG254

site_idAC7
Number of Residues12
DetailsBINDING SITE FOR RESIDUE LAB D1374
ChainResidue
DGLY15
DILE34
DTYR69
DASP157
DARG183
DTHR186
DARG206
DGLU207
DARG210
DLYS213
DATP1372
DHOH2097

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SCN B1376
ChainResidue
BGLY197
BSER199

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SCN D1375
ChainResidue
DGLY197
DSER199

site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SCN B1377
ChainResidue
BTRP79

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 Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:27304076
ChainResidueDetails
ESER98
FSER98

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylaspartate; in Actin, alpha skeletal muscle => ECO:0000269|PubMed:1150665
ChainResidueDetails
BASP1
DASP1

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134
ChainResidueDetails
BMET44
BMET47
DMET44
DMET47

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-malonyllysine => ECO:0000250
ChainResidueDetails
BLYS61
DLYS61

site_idSWS_FT_FI5
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_FI6
Number of Residues2
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133
ChainResidueDetails
BLYS84
DLYS84

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096
ChainResidueDetails
BARG177
DARG177

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PDB entries from 2024-07-17

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