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5TBY

HUMAN BETA CARDIAC HEAVY MEROMYOSIN INTERACTING-HEADS MOTIF OBTAINED BY HOMOLOGY MODELING (USING SWISS-MODEL) OF HUMAN SEQUENCE FROM APHONOPELMA HOMOLOGY MODEL (PDB-3JBH), RIGIDLY FITTED TO HUMAN BETA-CARDIAC NEGATIVELY STAINED THICK FILAMENT 3D-RECONSTRUCTION (EMD-2240)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000146molecular_functionmicrofilament motor activity
A0000166molecular_functionnucleotide binding
A0001725cellular_componentstress fiber
A0002026biological_processregulation of the force of heart contraction
A0002027biological_processregulation of heart rate
A0003009biological_processskeletal muscle contraction
A0003774molecular_functioncytoskeletal motor activity
A0003779molecular_functionactin binding
A0005515molecular_functionprotein binding
A0005516molecular_functioncalmodulin binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005859cellular_componentmuscle myosin complex
A0006936biological_processmuscle contraction
A0006941biological_processstriated muscle contraction
A0007512biological_processadult heart development
A0014728biological_processregulation of the force of skeletal muscle contraction
A0014883biological_processtransition between fast and slow fiber
A0014898biological_processcardiac muscle hypertrophy in response to stress
A0016459cellular_componentmyosin complex
A0016460cellular_componentmyosin II complex
A0030016cellular_componentmyofibril
A0030017cellular_componentsarcomere
A0030018cellular_componentZ disc
A0030049biological_processmuscle filament sliding
A0031449biological_processregulation of slow-twitch skeletal muscle fiber contraction
A0032982cellular_componentmyosin filament
A0045214biological_processsarcomere organization
A0046034biological_processATP metabolic process
A0051015molecular_functionactin filament binding
A0055010biological_processventricular cardiac muscle tissue morphogenesis
A0060048biological_processcardiac muscle contraction
B0000146molecular_functionmicrofilament motor activity
B0000166molecular_functionnucleotide binding
B0001725cellular_componentstress fiber
B0002026biological_processregulation of the force of heart contraction
B0002027biological_processregulation of heart rate
B0003009biological_processskeletal muscle contraction
B0003774molecular_functioncytoskeletal motor activity
B0003779molecular_functionactin binding
B0005515molecular_functionprotein binding
B0005516molecular_functioncalmodulin binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005859cellular_componentmuscle myosin complex
B0006936biological_processmuscle contraction
B0006941biological_processstriated muscle contraction
B0007512biological_processadult heart development
B0014728biological_processregulation of the force of skeletal muscle contraction
B0014883biological_processtransition between fast and slow fiber
B0014898biological_processcardiac muscle hypertrophy in response to stress
B0016459cellular_componentmyosin complex
B0016460cellular_componentmyosin II complex
B0030016cellular_componentmyofibril
B0030017cellular_componentsarcomere
B0030018cellular_componentZ disc
B0030049biological_processmuscle filament sliding
B0031449biological_processregulation of slow-twitch skeletal muscle fiber contraction
B0032982cellular_componentmyosin filament
B0045214biological_processsarcomere organization
B0046034biological_processATP metabolic process
B0051015molecular_functionactin filament binding
B0055010biological_processventricular cardiac muscle tissue morphogenesis
B0060048biological_processcardiac muscle contraction
C0002026biological_processregulation of the force of heart contraction
C0003785molecular_functionactin monomer binding
C0005509molecular_functioncalcium ion binding
C0005829cellular_componentcytosol
C0005859cellular_componentmuscle myosin complex
C0006936biological_processmuscle contraction
C0006942biological_processregulation of striated muscle contraction
C0008307molecular_functionstructural constituent of muscle
C0016459cellular_componentmyosin complex
C0016460cellular_componentmyosin II complex
C0030017cellular_componentsarcomere
C0031672cellular_componentA band
C0031674cellular_componentI band
C0032038molecular_functionmyosin II heavy chain binding
C0032781biological_processpositive regulation of ATP-dependent activity
C0055010biological_processventricular cardiac muscle tissue morphogenesis
C0060048biological_processcardiac muscle contraction
D0002026biological_processregulation of the force of heart contraction
D0003785molecular_functionactin monomer binding
D0005509molecular_functioncalcium ion binding
D0005829cellular_componentcytosol
D0005859cellular_componentmuscle myosin complex
D0006936biological_processmuscle contraction
D0006942biological_processregulation of striated muscle contraction
D0008307molecular_functionstructural constituent of muscle
D0016459cellular_componentmyosin complex
D0016460cellular_componentmyosin II complex
D0030017cellular_componentsarcomere
D0031672cellular_componentA band
D0031674cellular_componentI band
D0032038molecular_functionmyosin II heavy chain binding
D0032781biological_processpositive regulation of ATP-dependent activity
D0055010biological_processventricular cardiac muscle tissue morphogenesis
D0060048biological_processcardiac muscle contraction
E0002026biological_processregulation of the force of heart contraction
E0003785molecular_functionactin monomer binding
E0005509molecular_functioncalcium ion binding
E0005515molecular_functionprotein binding
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0005856cellular_componentcytoskeleton
E0006942biological_processregulation of striated muscle contraction
E0007507biological_processheart development
E0008307molecular_functionstructural constituent of muscle
E0015629cellular_componentactin cytoskeleton
E0016459cellular_componentmyosin complex
E0030016cellular_componentmyofibril
E0030017cellular_componentsarcomere
E0030308biological_processnegative regulation of cell growth
E0031672cellular_componentA band
E0032036molecular_functionmyosin heavy chain binding
E0042694biological_processmuscle cell fate specification
E0046872molecular_functionmetal ion binding
E0055003biological_processcardiac myofibril assembly
E0055010biological_processventricular cardiac muscle tissue morphogenesis
E0060047biological_processheart contraction
E0060048biological_processcardiac muscle contraction
E0097512cellular_componentcardiac myofibril
E0098735biological_processpositive regulation of the force of heart contraction
F0002026biological_processregulation of the force of heart contraction
F0003785molecular_functionactin monomer binding
F0005509molecular_functioncalcium ion binding
F0005515molecular_functionprotein binding
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0005856cellular_componentcytoskeleton
F0006942biological_processregulation of striated muscle contraction
F0007507biological_processheart development
F0008307molecular_functionstructural constituent of muscle
F0015629cellular_componentactin cytoskeleton
F0016459cellular_componentmyosin complex
F0030016cellular_componentmyofibril
F0030017cellular_componentsarcomere
F0030308biological_processnegative regulation of cell growth
F0031672cellular_componentA band
F0032036molecular_functionmyosin heavy chain binding
F0042694biological_processmuscle cell fate specification
F0046872molecular_functionmetal ion binding
F0055003biological_processcardiac myofibril assembly
F0055010biological_processventricular cardiac muscle tissue morphogenesis
F0060047biological_processheart contraction
F0060048biological_processcardiac muscle contraction
F0097512cellular_componentcardiac myofibril
F0098735biological_processpositive regulation of the force of heart contraction
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DQNRDGFIDknDL
ChainResidueDetails
EASP37-LEU49

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
ChainResidueDetails
EASP37
EASN39
EASP41
EASP48
FASP37
FASN39
FASP41
FASP48

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N,N,N-trimethylalanine => ECO:0000250|UniProtKB:P51667
ChainResidueDetails
EALA2
FALA2
DTHR88
DTHR129

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Deamidated asparagine => ECO:0000269|PubMed:20445002
ChainResidueDetails
EASN14
FASN14
ATHR1309
ATHR1513
BTHR378
BTHR1282
BTHR1309
BTHR1513

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine; by ZIPK/DAPK3 => ECO:0000269|PubMed:20038585, ECO:0000269|PubMed:20445002
ChainResidueDetails
ESER15
FSER15

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P51667
ChainResidueDetails
ESER19
FSER19

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P08733
ChainResidueDetails
ETHR52
FTHR52

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P02564
ChainResidueDetails
ASER1510
BSER1510

218853

PDB entries from 2024-04-24

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