Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7BTE

Lifeact-F-actin complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0001725cellular_componentstress fiber
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005865cellular_componentstriated muscle thin filament
A0005884cellular_componentactin filament
A0016787molecular_functionhydrolase activity
A0030240biological_processskeletal muscle thin filament assembly
A0048741biological_processskeletal muscle fiber development
C0001725cellular_componentstress fiber
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005856cellular_componentcytoskeleton
C0005865cellular_componentstriated muscle thin filament
C0005884cellular_componentactin filament
C0016787molecular_functionhydrolase activity
C0030240biological_processskeletal muscle thin filament assembly
C0048741biological_processskeletal muscle fiber development
E0001725cellular_componentstress fiber
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005737cellular_componentcytoplasm
E0005856cellular_componentcytoskeleton
E0005865cellular_componentstriated muscle thin filament
E0005884cellular_componentactin filament
E0016787molecular_functionhydrolase activity
E0030240biological_processskeletal muscle thin filament assembly
E0048741biological_processskeletal muscle fiber development
G0001725cellular_componentstress fiber
G0005515molecular_functionprotein binding
G0005524molecular_functionATP binding
G0005737cellular_componentcytoplasm
G0005856cellular_componentcytoskeleton
G0005865cellular_componentstriated muscle thin filament
G0005884cellular_componentactin filament
G0016787molecular_functionhydrolase activity
G0030240biological_processskeletal muscle thin filament assembly
G0048741biological_processskeletal muscle fiber development
I0001725cellular_componentstress fiber
I0005515molecular_functionprotein binding
I0005524molecular_functionATP binding
I0005737cellular_componentcytoplasm
I0005856cellular_componentcytoskeleton
I0005865cellular_componentstriated muscle thin filament
I0005884cellular_componentactin filament
I0016787molecular_functionhydrolase activity
I0030240biological_processskeletal muscle thin filament assembly
I0048741biological_processskeletal muscle fiber development
Functional Information from PDB Data
site_idAC1
Number of Residues1
Detailsbinding site for residue MG A 401
ChainResidue
AADP402

site_idAC2
Number of Residues12
Detailsbinding site for residue ADP A 402
ChainResidue
AGLY298
ATYR302
ALYS332
AMG401
AGLY9
ASER10
AGLY11
ALEU12
AGLY152
AASP153
ALYS209
AGLU210

site_idAC3
Number of Residues3
Detailsbinding site for residue MG C 801
ChainResidue
CGLN505
CASP522
CADP802

site_idAC4
Number of Residues15
Detailsbinding site for residue ADP C 802
ChainResidue
CGLY381
CSER382
CGLY383
CLEU384
CLYS386
CGLN505
CSER523
CGLY524
CASP525
CGLU582
CGLY670
CTHR671
CTYR674
CLYS704
CMG801

site_idAC5
Number of Residues2
Detailsbinding site for residue MG E 1201
ChainResidue
EGLN877
EADP1202

site_idAC6
Number of Residues12
Detailsbinding site for residue ADP E 1202
ChainResidue
EGLY753
ESER754
ELEU756
ELYS758
EGLY896
EASP897
EGLU954
EGLY1042
ETHR1043
ETYR1046
ELYS1076
EMG1201

site_idAC7
Number of Residues2
Detailsbinding site for residue MG G 1501
ChainResidue
GLYS1130
GADP1502

site_idAC8
Number of Residues13
Detailsbinding site for residue ADP G 1502
ChainResidue
GGLY1125
GSER1126
GGLY1127
GLEU1128
GLYS1130
GGLN1249
GGLY1268
GASP1269
GGLU1326
GGLY1414
GTYR1418
GLYS1448
GMG1501

site_idAC9
Number of Residues3
Detailsbinding site for residue MG I 1901
ChainResidue
IGLY1640
IASP1641
IADP1902

site_idAD1
Number of Residues10
Detailsbinding site for residue ADP I 1902
ChainResidue
IGLY1497
ILEU1500
IGLY1640
IASP1641
ILYS1697
IGLU1698
IGLY1786
ITYR1790
ILYS1820
IMG1901

Functional Information from PROSITE/UniProt
site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. YVGDEAQs.KRG
ChainResidueDetails
ATYR49-GLY59

site_idPS00432
Number of Residues9
DetailsACTINS_2 Actins signature 2. WITKqEYDE
ChainResidueDetails
ATRP352-GLU360

site_idPS01132
Number of Residues13
DetailsACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR
ChainResidueDetails
ALEU100-ARG112

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsMOD_RES: N-acetylcysteine; in intermediate form => ECO:0000250|UniProtKB:P62737
ChainResidueDetails
ACYS-4
CCYS368
ECYS740
GCYS1112
ICYS1484

site_idSWS_FT_FI2
Number of Residues5
DetailsMOD_RES: N-acetylaspartate; in Actin, alpha skeletal muscle => ECO:0000269|PubMed:456601
ChainResidueDetails
AASP-3
CASP369
EASP741
GASP1113
IASP1485

site_idSWS_FT_FI3
Number of Residues10
DetailsMOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134
ChainResidueDetails
AMET40
IMET1531
AMET43
CMET412
CMET415
EMET784
EMET787
GMET1156
GMET1159
IMET1528

site_idSWS_FT_FI4
Number of Residues5
DetailsMOD_RES: Tele-methylhistidine => ECO:0000269|PubMed:12356759, ECO:0007744|PDB:1MDU
ChainResidueDetails
AHIS69
CHIS441
EHIS813
GHIS1185
IHIS1557

site_idSWS_FT_FI5
Number of Residues5
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133
ChainResidueDetails
ALYS80
CLYS452
ELYS824
GLYS1196
ILYS1568

223790

PDB entries from 2024-08-14

PDB statisticsPDBj update infoContact PDBjnumon