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5YPU

Crystal structure of an actin monomer in complex with the nucleator Cordon-Bleu MET72NLE WH2-motif peptide

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
B0003779molecular_functionactin binding
C0000287molecular_functionmagnesium ion binding
C0001725cellular_componentstress fiber
C0003785molecular_functionactin monomer binding
C0005509molecular_functioncalcium ion binding
C0005515molecular_functionprotein binding
C0005523molecular_functiontropomyosin binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005856cellular_componentcytoskeleton
C0005865cellular_componentstriated muscle thin filament
C0005884cellular_componentactin filament
C0010628biological_processpositive regulation of gene expression
C0016787molecular_functionhydrolase activity
C0019904molecular_functionprotein domain specific binding
C0030027cellular_componentlamellipodium
C0030041biological_processactin filament polymerization
C0030175cellular_componentfilopodium
C0030240biological_processskeletal muscle thin filament assembly
C0031013molecular_functiontroponin I binding
C0031432molecular_functiontitin binding
C0031941cellular_componentfilamentous actin
C0032036molecular_functionmyosin heavy chain binding
C0032432cellular_componentactin filament bundle
C0042802molecular_functionidentical protein binding
C0044297cellular_componentcell body
C0048306molecular_functioncalcium-dependent protein binding
C0048741biological_processskeletal muscle fiber development
C0051017biological_processactin filament bundle assembly
C0090131biological_processmesenchyme migration
C0098723cellular_componentskeletal muscle myofibril
C0140660molecular_functioncytoskeletal motor activator activity
D0003779molecular_functionactin binding
Functional Information from PDB Data
site_idAC1
Number of Residues27
Detailsbinding site for residue ATP A 401
ChainResidue
AGLY13
AGLY182
AARG210
ALYS213
AGLU214
AGLY301
AGLY302
ATHR303
AMET305
ATYR306
ACA402
ASER14
AHOH586
AHOH604
AHOH615
AHOH627
AHOH634
AHOH660
AHOH689
AHOH708
AGLY15
ALEU16
ALYS18
AGLY156
AASP157
AGLY158
AVAL159

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 402
ChainResidue
AATP401
AHOH541
AHOH565
AHOH576
AHOH615
AHOH708

site_idAC3
Number of Residues6
Detailsbinding site for residue CA A 403
ChainResidue
AASP286
AASP288
AASP363
AHOH569
AHOH674
AHOH678

site_idAC4
Number of Residues7
Detailsbinding site for residue CA B 101
ChainResidue
AASP187
AHOH573
AHOH717
AHOH730
BGLU82
BHOH208
BHOH213

site_idAC5
Number of Residues27
Detailsbinding site for residue ATP C 401
ChainResidue
CGLY13
CSER14
CGLY15
CLEU16
CLYS18
CGLY156
CASP157
CGLY158
CVAL159
CGLY182
CARG210
CLYS213
CGLU214
CGLY301
CGLY302
CTHR303
CMET305
CTYR306
CCA402
CHOH574
CHOH586
CHOH589
CHOH599
CHOH604
CHOH611
CHOH622
CHOH680

site_idAC6
Number of Residues6
Detailsbinding site for residue CA C 402
ChainResidue
CATP401
CHOH539
CHOH552
CHOH559
CHOH586
CHOH622

site_idAC7
Number of Residues6
Detailsbinding site for residue CA C 403
ChainResidue
CASP286
CASP288
CASP363
CHOH571
CHOH674
CHOH675

site_idAC8
Number of Residues6
Detailsbinding site for residue CA C 404
ChainResidue
AHOH581
AHOH748
CASP288
CASP363
CHOH571
CHOH662

site_idAC9
Number of Residues6
Detailsbinding site for residue CA D 101
ChainResidue
CASP187
CHOH505
DGLU82
DHOH209
DHOH210
DHOH212

site_idAD1
Number of Residues10
Detailsbinding site for Di-peptide LEU D 71 and NLE D 72
ChainResidue
DLEU67
DHIS68
DSER69
DALA70
DGLU73
DALA74
DILE75
DHIS76
CTHR351
CMET355

site_idAD2
Number of Residues9
Detailsbinding site for Di-peptide NLE D 72 and GLU D 73
ChainResidue
DHIS68
DSER69
DALA70
DLEU71
DALA74
DILE75
DHIS76
DSER77
DHOH201

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
DetailsMOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134
ChainResidueDetails
AMET44
AMET47
CMET44
CMET47

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-malonyllysine => ECO:0000250
ChainResidueDetails
ALYS61
CLYS61

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
AHIS73
CHIS73

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133
ChainResidueDetails
ALYS84
CLYS84

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096
ChainResidueDetails
AARG177
CARG177

220113

PDB entries from 2024-05-22

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