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

6C1D

High-Resolution Cryo-EM Structures of Actin-bound Myosin States Reveal the Mechanism of Myosin Force Sensing

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
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
B0000166molecular_functionnucleotide binding
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
C0000166molecular_functionnucleotide 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
D0000166molecular_functionnucleotide binding
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
E0000166molecular_functionnucleotide binding
E0000287molecular_functionmagnesium ion binding
E0001725cellular_componentstress fiber
E0003785molecular_functionactin monomer binding
E0005509molecular_functioncalcium ion binding
E0005515molecular_functionprotein binding
E0005523molecular_functiontropomyosin binding
E0005524molecular_functionATP binding
E0005737cellular_componentcytoplasm
E0005856cellular_componentcytoskeleton
E0005865cellular_componentstriated muscle thin filament
E0005884cellular_componentactin filament
E0010628biological_processpositive regulation of gene expression
E0016787molecular_functionhydrolase activity
E0019904molecular_functionprotein domain specific binding
E0030027cellular_componentlamellipodium
E0030041biological_processactin filament polymerization
E0030175cellular_componentfilopodium
E0030240biological_processskeletal muscle thin filament assembly
E0031013molecular_functiontroponin I binding
E0031432molecular_functiontitin binding
E0031941cellular_componentfilamentous actin
E0032036molecular_functionmyosin heavy chain binding
E0032432cellular_componentactin filament bundle
E0042802molecular_functionidentical protein binding
E0044297cellular_componentcell body
E0048306molecular_functioncalcium-dependent protein binding
E0048741biological_processskeletal muscle fiber development
E0051017biological_processactin filament bundle assembly
E0090131biological_processmesenchyme migration
E0098723cellular_componentskeletal muscle myofibril
E0140660molecular_functioncytoskeletal motor activator activity
P0003774molecular_functioncytoskeletal motor activity
P0005524molecular_functionATP binding
P0016459cellular_componentmyosin complex
R0000086biological_processG2/M transition of mitotic cell cycle
R0000922cellular_componentspindle pole
R0002027biological_processregulation of heart rate
R0005509molecular_functioncalcium ion binding
R0005513biological_processdetection of calcium ion
R0005515molecular_functionprotein binding
R0005576cellular_componentextracellular region
R0005634cellular_componentnucleus
R0005654cellular_componentnucleoplasm
R0005737cellular_componentcytoplasm
R0005813cellular_componentcentrosome
R0005819cellular_componentspindle
R0005829cellular_componentcytosol
R0005856cellular_componentcytoskeleton
R0005876cellular_componentspindle microtubule
R0005886cellular_componentplasma membrane
R0005929cellular_componentcilium
R0007186biological_processG protein-coupled receptor signaling pathway
R0008076cellular_componentvoltage-gated potassium channel complex
R0010800biological_processpositive regulation of peptidyl-threonine phosphorylation
R0010801biological_processnegative regulation of peptidyl-threonine phosphorylation
R0010856molecular_functionadenylate cyclase activator activity
R0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
R0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
R0016020cellular_componentmembrane
R0016240biological_processautophagosome membrane docking
R0019855molecular_functioncalcium channel inhibitor activity
R0019901molecular_functionprotein kinase binding
R0021762biological_processsubstantia nigra development
R0030017cellular_componentsarcomere
R0030234molecular_functionenzyme regulator activity
R0031432molecular_functiontitin binding
R0031514cellular_componentmotile cilium
R0031954biological_processpositive regulation of protein autophosphorylation
R0031982cellular_componentvesicle
R0032465biological_processregulation of cytokinesis
R0032516biological_processpositive regulation of phosphoprotein phosphatase activity
R0032991cellular_componentprotein-containing complex
R0034704cellular_componentcalcium channel complex
R0035307biological_processpositive regulation of protein dephosphorylation
R0035458biological_processcellular response to interferon-beta
R0042995cellular_componentcell projection
R0043209cellular_componentmyelin sheath
R0043539molecular_functionprotein serine/threonine kinase activator activity
R0044325molecular_functiontransmembrane transporter binding
R0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
R0046872molecular_functionmetal ion binding
R0048306molecular_functioncalcium-dependent protein binding
R0050848biological_processregulation of calcium-mediated signaling
R0051343biological_processpositive regulation of cyclic-nucleotide phosphodiesterase activity
R0051592biological_processresponse to calcium ion
R0055117biological_processregulation of cardiac muscle contraction
R0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
R0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
R0060316biological_processpositive regulation of ryanodine-sensitive calcium-release channel activity
R0071346biological_processcellular response to type II interferon
R0071902biological_processpositive regulation of protein serine/threonine kinase activity
R0072542molecular_functionprotein phosphatase activator activity
R0097225cellular_componentsperm midpiece
R0098901biological_processregulation of cardiac muscle cell action potential
R0140056biological_processorganelle localization by membrane tethering
R1901842biological_processnegative regulation of high voltage-gated calcium channel activity
R1901844biological_processregulation of cell communication by electrical coupling involved in cardiac conduction
R1902494cellular_componentcatalytic complex
R1905913biological_processnegative regulation of calcium ion export across plasma membrane
R1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue ADP A 401
ChainResidue
AGLY13
AGLU214
AGLY302
ATHR303
AMET305
ALYS336
AMG402
ASER14
AGLY15
ALEU16
ALYS18
AGLY156
AASP157
AARG210
ALYS213

site_idAC2
Number of Residues2
Detailsbinding site for residue MG A 402
ChainResidue
AGLN137
AADP401

site_idAC3
Number of Residues15
Detailsbinding site for residue ADP B 401
ChainResidue
BGLY13
BSER14
BGLY15
BLEU16
BLYS18
BGLY156
BASP157
BARG210
BLYS213
BGLU214
BGLY302
BTHR303
BMET305
BLYS336
BMG402

site_idAC4
Number of Residues2
Detailsbinding site for residue MG B 402
ChainResidue
BGLN137
BADP401

site_idAC5
Number of Residues15
Detailsbinding site for residue ADP C 401
ChainResidue
CGLY13
CSER14
CGLY15
CLEU16
CLYS18
CGLY156
CASP157
CARG210
CLYS213
CGLU214
CGLY302
CTHR303
CMET305
CLYS336
CMG402

site_idAC6
Number of Residues2
Detailsbinding site for residue MG C 402
ChainResidue
CGLN137
CADP401

site_idAC7
Number of Residues14
Detailsbinding site for residue ADP D 401
ChainResidue
DGLY13
DSER14
DGLY15
DLEU16
DLYS18
DGLY156
DASP157
DARG210
DLYS213
DGLU214
DGLY302
DTHR303
DLYS336
DMG402

site_idAC8
Number of Residues2
Detailsbinding site for residue MG D 402
ChainResidue
DGLN137
DADP401

site_idAC9
Number of Residues14
Detailsbinding site for residue ADP E 401
ChainResidue
EGLY13
ESER14
EGLY15
ELEU16
ELYS18
EGLY156
EASP157
EARG210
ELYS213
EGLU214
EGLY302
ETHR303
ELYS336
EMG402

site_idAD1
Number of Residues2
Detailsbinding site for residue MG E 402
ChainResidue
EGLN137
EADP401

site_idAD2
Number of Residues2
Detailsbinding site for residue MG P 801
ChainResidue
PTHR115
PADP802

site_idAD3
Number of Residues2
Detailsbinding site for residue ADP P 802
ChainResidue
PASN162
PMG801

Functional Information from PROSITE/UniProt
site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. YVGDEAQs.KRG
ChainResidueDetails
ATYR53-GLY63

site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
RASP20-LEU32
RASP56-PHE68
RASP93-LEU105
RASP129-PHE141

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 Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
ChainResidueDetails
RASP20
RGLU67
RASP22
RASP24
RTHR26
RGLU31
RASP56
RASP58
RASN60
RTHR62

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
ChainResidueDetails
RASP93
RGLU140
RASP95
RASN97
RTYR99
RGLU104
RASP129
RASP131
RASP133
RGLN135

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:7093203, ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
ChainResidueDetails
RALA1
BLYS61
CLYS61
DLYS61
ELYS61

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
RLYS21
BHIS73
CHIS73
DHIS73
EHIS73

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29
ChainResidueDetails
RTHR44
BLYS84
CLYS84
DLYS84
ELYS84

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
RSER81
BARG177
CARG177
DARG177
EARG177

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
RLYS94

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332
ChainResidueDetails
RTYR99

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
RSER101

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
RTHR110

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0007744|PubMed:24129315
ChainResidueDetails
RLYS115

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332
ChainResidueDetails
RTYR138

site_idSWS_FT_FI13
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157
ChainResidueDetails
RLYS21

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon