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Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：Q14896 New Search
17PDB entries
17Biological assembly
70chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
1GXE Central domain of cardiac myosin binding protein C Deposited 2002-04-03 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
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 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
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 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
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 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
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 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
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 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
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 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
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 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric（20） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric（20） Consistent with protein count
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
6G2T human cardiac myosin binding protein C C1 Ig-domain bound to native cardiac thin filament Deposited 2018-03-23 Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein count
Chain G 151–258（108 aa）
Chain H 151–258（108 aa）
Chain I 151–258（108 aa）
Chain J 151–258（108 aa）
Chain K 151–258（108 aa）
Chain L 151–258（108 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 9.00 Å
7LRG Filamentous actin decorated with human cardiac myosin binding protein C C2 domain Deposited 2021-02-16 Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric（12） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric（12） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 22 PDB declaration: 22-meric（22） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 123 PDB declaration: 123-meric（123） Consistent with protein count
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

This page presents structural evidence recorded in PDB/mmCIF.“No recorded non-water small molecule” does not prove that the experimental sample was ligand-free; experimental conditions belong to the PDB experiment, while ligands and copy counts are shown for each biological assembly.