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6g2t

human cardiac myosin binding protein C C1 Ig-domain bound to native cardiac thin filament

Method: ELECTRON MICROSCOPY Dmax: 209.2 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Actin, cytoplasmic 2

Homo sapiens

UniProt P63261

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein copy count Chain A； UniProt 1–375 Chain B； UniProt 1–375 Chain C； UniProt 1–375 Chain D； UniProt 1–375 Chain E； UniProt 1–375 Chain F； UniProt 1–375 Not recorded Myosin-binding protein C, cardiac-type × 6 （Q14896） Tropomyosin × 4 ELECTRON MICROSCOPY cryo-EM buffer：pH 7 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 9.00 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 6G2T Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
5JLH Cryo-EM structure of a human cytoplasmic actomyosin complex at near-atomic resolution Deposited 2016-04-27 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 11 PDB declaration: undecameric
Chain A 2–375（374 aa）
Chain B 2–375（374 aa）
Chain C 2–375（374 aa）
Chain D 2–375（374 aa）
Chain E 2–375（374 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 5 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5；5 mM Tris-HCl pH 7.5, 1 mM DTT, 100 mM KCl, and 2 mM MgCl2
cryo-EM vitrification conditions Cryogen ETHANE；Sample (2 uL of F-actin-tropomyosin solution) was applied to a glow-discharged holey carbon grid, incubated for 20 s and manually blotted from the backside for less than a second with filter paper. Afterwards 1.5 uL of myosin solution (3 uM without nucleotide) were added directly on the grid, incubated for 10 s and then manually blotted for 5 s from the backside with filter paper.
Resolution 3.90 Å
6CXI Cardiac thin filament decorated with C0C1 fragment of cardiac myosin binding protein C mode 1 Deposited 2018-04-03 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain A 1–375（375 aa）
Chain B 1–375（375 aa）
Chain C 1–375（375 aa）
Chain D 1–375（375 aa）
Chain E 1–375（375 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 11.00 Å
6CXJ Cardiac thin filament decorated with C0C1 fragment of cardiac myosin binding protein C mode 2 Deposited 2018-04-03 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain A 1–375（375 aa）
Chain B 1–375（375 aa）
Chain C 1–375（375 aa）
Chain D 1–375（375 aa）
Chain E 1–375（375 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 11.00 Å
6WK1 SETD3 in Complex with an Actin Peptide with His73 Replaced with Methionine Deposited 2020-04-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain Y 66–88（23 aa）
Chain Z 66–88（23 aa）
Mutation：H73M Mutation：H73M GOL GLYCEROL × 6 EDO 1,2-ETHANEDIOL × 46 SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 ACT ACETATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；292 K；0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate pH 5.6 and 30% (w/v) polyethylene glycol 4000
Resolution 1.89 Å R-free 0.228
6WK1 SETD3 in Complex with an Actin Peptide with His73 Replaced with Methionine Deposited 2020-04-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain Y 66–88（23 aa）
Mutation：H73M GOL GLYCEROL × 6 EDO 1,2-ETHANEDIOL × 27 SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 ACT ACETATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；292 K；0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate pH 5.6 and 30% (w/v) polyethylene glycol 4000
Resolution 1.89 Å R-free 0.228
6WK1 SETD3 in Complex with an Actin Peptide with His73 Replaced with Methionine Deposited 2020-04-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain Z 66–88（23 aa）
Mutation：H73M EDO 1,2-ETHANEDIOL × 19 SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；292 K；0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate pH 5.6 and 30% (w/v) polyethylene glycol 4000
Resolution 1.89 Å R-free 0.228
6WK2 SETD3 mutant (N255V) in Complex with an Actin Peptide with His73 Replaced with Methionine Deposited 2020-04-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 66–88（23 aa）
Chain Y 66–88（23 aa）
Mutation：H73M Mutation：H73M SAM S-ADENOSYLMETHIONINE × 2 EDO 1,2-ETHANEDIOL × 8 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；292 K；0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate pH 5.6 and 30% (w/v) polyethylene glycol 4000
Resolution 1.76 Å R-free 0.206
6WK2 SETD3 mutant (N255V) in Complex with an Actin Peptide with His73 Replaced with Methionine Deposited 2020-04-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain Y 66–88（23 aa）
Mutation：H73M SAM S-ADENOSYLMETHIONINE × 1 EDO 1,2-ETHANEDIOL × 7 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；292 K；0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate pH 5.6 and 30% (w/v) polyethylene glycol 4000
Resolution 1.76 Å R-free 0.206
6WK2 SETD3 mutant (N255V) in Complex with an Actin Peptide with His73 Replaced with Methionine Deposited 2020-04-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 66–88（23 aa）
Mutation：H73M SAM S-ADENOSYLMETHIONINE × 1 EDO 1,2-ETHANEDIOL × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；292 K；0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate pH 5.6 and 30% (w/v) polyethylene glycol 4000
Resolution 1.76 Å R-free 0.206
7NVM Human TRiC complex in closed state with nanobody Nb18, actin and PhLP2A bound Deposited 2021-03-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain K 1–375（375 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 16 MG MAGNESIUM ION × 16 AF3 ALUMINUM FLUORIDE × 16 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.10 Å
8DNF Cryo-EM structure of nonmuscle gamma-actin Deposited 2022-07-11 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–375（374 aa）
Chain B 2–375（374 aa）
Chain C 2–375（374 aa）
Chain D 2–375（374 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.38 Å
9SMX CM1-activated gTuRC in complex with nascent alpha-E254D mutant microtubules Deposited 2025-09-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 73 PDB declaration: 73-meric
Chain 7 2–375（374 aa）
Not recorded GTP GUANOSINE-5'-TRIPHOSPHATE × 11 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.9
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.67 Å

8 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTG_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–375； UniProt 1–375 Author chain B； PDBConstruct 1–375； UniProt 1–375 Author chain C； PDBConstruct 1–375； UniProt 1–375 Author chain D； PDBConstruct 1–375； UniProt 1–375 Author chain E； PDBConstruct 1–375； UniProt 1–375 Author chain F； PDBConstruct 1–375； UniProt 1–375

Myosin-binding protein C, cardiac-type

Homo sapiens

UniProt Q14896

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein copy count Chain G； UniProt 151–258 Chain H； UniProt 151–258 Chain I； UniProt 151–258 Chain J； UniProt 151–258 Chain K； UniProt 151–258 Chain L； UniProt 151–258 Not recorded Actin, cytoplasmic 2 × 6 （P63261） Tropomyosin × 4 ELECTRON MICROSCOPY cryo-EM buffer：pH 7 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 9.00 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 6G2T Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1GXE Central domain of cardiac myosin binding protein C Deposited 2002-04-03 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 641–770（130 aa） Fragment：DOMAIN C5, RESIDUES 641-770
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；293 K；Ionic strength (raw mmCIF value) 100 MM NACL；Pressure 1
Resolution not provided
1PD6 The NMR structure of domain C2 of human cardiac Myosin Binding Protein C Deposited 2003-05-19 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 358–451（94 aa） Fragment：Domain C2
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 0.1；Pressure ambient
NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 0.1；Pressure ambient
NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 7.0；Pressure ambient
NMR sample composition 0.75mM C2; 15N; 20mM phosphate buffer; 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 0.75mM C2; 15N, 13C; 20mM phosphate buffer; 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 0.75mM C2; 15N, 13C; 20mM phosphate buffer; 100% D2O | 100% D2O
Resolution not provided
2AVG NMR structure of cC1 domain from Human Cardiac Myosin Binding Protein C Deposited 2005-08-30 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 151–260（110 aa） Fragment：cC1 domain
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 0.1M；Pressure ambient
NMR sample composition 0.8mM cC1 U-15N; 20mM phosphate buffer; 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 0.8mM cC1 U-15N, 13C; 20mM phosphate buffer; 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 0.8mM cC1 U-15N, 13C; 20mM phosphate buffer; 100% D2O | 100% D2O
Resolution not provided
2K1M 3D NMR structure of domain cC0 of cardiac myosin binding protein C (MyBPC) Deposited 2008-03-10 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2–96（95 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；303 K；Ionic strength (raw mmCIF value) 185；Pressure ambient
NMR sample composition 1-1.5 mM [U-95% 13C; U-95% 15N] cC0_MyBPC, 55.5 M [U-2H] D2O, 40 mM sodium phosphate, 50 mM sodium chloride, 2 mM DTT, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1-1.5 mM [U-95% 15N] cC0_MyBPC, 55.5 M H2O, 40 mM sodium phosphate, 50 mM sodium chloride, 2 mM DTT, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1-1.5 mM cC0_MyBPC, 55.5 M H2O, 40 mM sodium phosphate, 50 mM sodium chloride, 2 mM DTT, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
2MQ0 NMR structure of the c3 domain of human cardiac myosin binding protein-c Deposited 2014-06-10 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 453–543（91 aa） Fragment：unp residues 453-543
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 0.4；Pressure ambient
NMR sample composition 50 mM sodium phosphate, 100 mM sodium chloride, 0.8 mM [U-100% 13C; U-100% 15N] protein, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
2MQ3 NMR structure of the c3 domain of human cardiac myosin binding protein-c with a hypertrophic cardiomyopathy-related mutation R502W. Deposited 2014-06-12 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 453–543（91 aa） Fragment：unp residues 453-543
Mutation：R502W No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 0.4；Pressure ambient
NMR sample composition 50 mM sodium phosphate, 100 mM sodium chloride, 0.8 mM [U-100% 13C; U-100% 15N] protein, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
2V6H Crystal structure of the C1 domain of cardiac myosin binding protein-C Deposited 2007-07-18 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 151–258（108 aa） Fragment：C1 DOMAIN, RESIDUES 151-258
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.3；293 K；HANGING DROP; 20 C; 18%PEG, 0.1M BUFFER, PH 7.3
Resolution 1.55 Å R-free 0.241
3CX2 Crystal structure of the C1 domain of cardiac isoform of myosin binding protein-C at 1.3A Deposited 2008-04-23 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 151–258（108 aa） Fragment：Ig-like C2-type 1 domain
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.9；293 K；Crystals were grown at 20 C using the hanging drop method with a 2 microlitre drop containing a 1:1 mixture of protein solution and crystallising solution consisting of 8.5% PEG 3350 and 0.05M Hepes pH 6.8 over 500 microlitres of crystallising solution in the reservoir, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.30 Å R-free 0.209
5K6P The NMR structure of the m domain tri-helix bundle and C2 of human cardiac Myosin Binding Protein C Deposited 2016-05-25 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 319–451（133 aa） Fragment：residues 319-451
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 50；Pressure 1
NMR sample composition 412 uM [U-99% 13C; U-99% 15N] human cMyBP-C (319-451), 10 mM MES, 1 mM CaCl2, 50 mM NaCl, 2 mM TCEP, 1 mM Na azide, 10 mM DSS, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 920 uM [U-99% 13C; U-99% 15N] human cMyBP-C (319-451), 10 mM MES, 1 mM CaCl2, 50 mM NaCl, 2 mM TCEP, 1 mM Na azide, 10 mM DSS, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 550 uM [U-99% 13C; U-99% 15N] human cMyBP-C (319-451), 10 mM MES, 1 mM CaCl2, 50 mM NaCl, 1 mM Na azide, 2 mM TCEP, 10 mM DSS, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 500 uM [U-99% 13C; U-99% 15N] human cMyBP-C (319-451), 10 mM MES, 1 mM CaCl2, 50 mM NaCl, 2 mM TCEP, 1 mM Na azide, 10 mM DSS, 99% D2O | 99% D2O
NMR sample composition 800 uM [U-99% 13C; U-99% 15N] human cMyBP-C (319-451), 10 mM MES, 1 mM CaCl2, 50 mM NaCl, 2 mM TCEP, 1 mM Na azide, 10 mM DSS, 99% D2O | 99% D2O
Resolution not provided
6CXI Cardiac thin filament decorated with C0C1 fragment of cardiac myosin binding protein C mode 1 Deposited 2018-04-03 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain G 151–258（108 aa） Fragment：C1 Ig-domain (UNP residues 151-258)
Chain H 151–258（108 aa） Fragment：C1 Ig-domain (UNP residues 151-258)
Chain I 151–258（108 aa） Fragment：C1 Ig-domain (UNP residues 151-258)
Chain J 151–258（108 aa） Fragment：C1 Ig-domain (UNP residues 151-258)
Chain K 151–258（108 aa） Fragment：C1 Ig-domain (UNP residues 151-258)
Chain L 151–258（108 aa） Fragment：C1 Ig-domain (UNP residues 151-258)
Chain M 1–101（101 aa） Fragment：C0 Ig-domain (UNP residues 1-101)
Chain N 1–101（101 aa） Fragment：C0 Ig-domain (UNP residues 1-101)
Chain O 1–101（101 aa） Fragment：C0 Ig-domain (UNP residues 1-101)
Chain P 1–101（101 aa） Fragment：C0 Ig-domain (UNP residues 1-101)
Chain Q 1–101（101 aa） Fragment：C0 Ig-domain (UNP residues 1-101)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 11.00 Å
6CXJ Cardiac thin filament decorated with C0C1 fragment of cardiac myosin binding protein C mode 2 Deposited 2018-04-03 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain G 151–258（108 aa） Fragment：C1 Ig-domain (UNP residues 151-258)
Chain H 151–258（108 aa） Fragment：C1 Ig-domain (UNP residues 151-258)
Chain I 151–258（108 aa） Fragment：C1 Ig-domain (UNP residues 151-258)
Chain J 151–258（108 aa） Fragment：C1 Ig-domain (UNP residues 151-258)
Chain K 151–258（108 aa） Fragment：C1 Ig-domain (UNP residues 151-258)
Chain L 151–258（108 aa） Fragment：C1 Ig-domain (UNP residues 151-258)
Chain M 1–101（101 aa） Fragment：C0 Ig-domain (UNP residues 1-101)
Chain N 1–101（101 aa） Fragment：C0 Ig-domain (UNP residues 1-101)
Chain O 1–101（101 aa） Fragment：C0 Ig-domain (UNP residues 1-101)
Chain P 1–101（101 aa） Fragment：C0 Ig-domain (UNP residues 1-101)
Chain Q 1–101（101 aa） Fragment：C0 Ig-domain (UNP residues 1-101)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 11.00 Å
7LRG Filamentous actin decorated with human cardiac myosin binding protein C C2 domain Deposited 2021-02-16 Different construct Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain G 358–451（94 aa）
Chain H 358–451（94 aa）
Chain I 358–451（94 aa）
Chain J 358–451（94 aa）
Chain K 358–451（94 aa）
Chain L 358–451（94 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 6.10 Å
7TIJ Cardiac F-actin decorated with regulatory M-domain of cardiac myosin binding protein C Deposited 2022-01-13 Different construct Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain G 151–370（220 aa）
Chain H 151–370（220 aa）
Chain I 151–370（220 aa）
Chain J 151–370（220 aa）
Chain K 151–370（220 aa）
Chain L 151–370（220 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 8.00 Å
7TIT Cardiac thin filament decorated with regulatory M-domain of cardiac myosin binding protein C Deposited 2022-01-14 Different construct Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric
Chain G 151–370（220 aa）
Chain H 151–370（220 aa）
Chain I 151–370（220 aa）
Chain J 151–370（220 aa）
Chain K 151–370（220 aa）
Chain L 151–370（220 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 8.00 Å
7TJ7 Cardiac thin filament decorated with C1 Ig-domain and regulatory M-domain of cardiac myosin binding protein C (cMyBP-C) Deposited 2022-01-14 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 22 PDB declaration: 22-meric
Chain G 151–370（220 aa）
Chain H 151–370（220 aa）
Chain I 151–370（220 aa）
Chain J 151–370（220 aa）
Chain K 151–370（220 aa）
Chain L 151–370（220 aa）
Chain M 151–370（220 aa）
Chain N 151–370（220 aa）
Chain O 151–370（220 aa）
Chain P 151–370（220 aa）
Chain Q 151–370（220 aa）
Chain R 151–370（220 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 8.00 Å
8G4L Cryo-EM structure of the human cardiac myosin filament Deposited 2023-02-10 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 123 PDB declaration: 123-meric
Chain ao 1–1274（1274 aa）
Chain bo 1–1274（1274 aa）
Chain o 1–1274（1274 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 6.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 6.40 Å

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MYPC3_HUMAN
Isoform Q14896-2
PDB entities 2
Chains and sequence ranges Author chain G； PDBConstruct 2–109； UniProt 151–258 Author chain H； PDBConstruct 2–109； UniProt 151–258 Author chain I； PDBConstruct 2–109； UniProt 151–258 Author chain J； PDBConstruct 2–109； UniProt 151–258 Author chain K； PDBConstruct 2–109； UniProt 151–258 Author chain L； PDBConstruct 2–109； UniProt 151–258

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 6g2t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6g2t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6g2t
Deposition date deposition_date2018-03-23
Structure title titlehuman cardiac myosin binding protein C C1 Ig-domain bound to native cardiac thin filament
Keywords keywordsCardiac thin filament regulator, CONTRACTILE PROTEIN; CONTRACTILE PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier57.49 Å
Radius of gyration Rg (electron density) rg_electron57.65 Å
Forward intensity I(0) i01876680000.00
Molecular weight molecular_weight354710.0 kDa
Excluded volume excluded_volume440530 ų
Envelope volume envelope_volume703210 ų
Hydration-shell volume shell_volume104640 ų
Envelope diameter envelope_diameter248.9 Å
Shell Rg shell_rg56.62 Å
Envelope Rg envelope_rg57.87 Å
Shape Rg shape_rg57.70 Å
Total Rg total_rg57.45 Å
Total atoms total_atoms24958
Residues n_residues3384
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax209.2 Å
Rg (real space) rg_real57.93 Å
Rg uncertainty (real space) rg_real_error1.70 Å
I(0) (real space) i0_real1.8760e+09
I(0) uncertainty (real space) i0_real_error3.6960e+07
Rg (reciprocal space) rg_reciprocal57.07 Å
I(0) (reciprocal space) i0_reciprocal1874000000.0000
Solution quality estimate total_estimate0.7999
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary54.2 Å
Skewness Skewness skewness0.630
Kurtosis Kurtosis kurtosis-0.025
Angular range angular_range— – 0.1350 Å−1
Current regularization parameter α current_alpha0.0073
Highest regularization parameter α highest_alpha524000000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.561; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.898; Smooth: 0.813
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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8. Citations (1)

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9. Files and Curves (10)