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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：P09493 New Search
14PDB entries
15Biological assembly
60chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion 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
3MUD Structure of the Tropomyosin Overlap Complex from Chicken Smooth Muscle Deposited 2010-05-02 Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain C 1–29（29 aa）
Chain D 1–29（29 aa）
Not recorded EDO 1,2-ETHANEDIOL × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；18% MePEG 2000, 100 mM Bis-Tris, 120 mM MgSO4 , pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.20 Å R-free 0.250
5KHT Crystal structure of the N-terminal fragment of tropomyosin isoform Tpm1.1 at 1.5 A resolution Deposited 2016-06-15 Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–28（28 aa）
Chain C 1–28（28 aa）
Not recorded PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；PEG 8000, Hepes/sodium hydroxide
Resolution 1.50 Å R-free 0.249
5KHT Crystal structure of the N-terminal fragment of tropomyosin isoform Tpm1.1 at 1.5 A resolution Deposited 2016-06-15 Assembly 2 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 1–28（28 aa）
Chain D 1–28（28 aa）
Not recorded PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；PEG 8000, Hepes/sodium hydroxide
Resolution 1.50 Å R-free 0.249
6KN7 Structure of human cardiac thin filament in the calcium free state Deposited 2019-08-03 Assembly 1 Protein heterocomplex Heteromer；Protein × 29 PDB declaration: 29-meric（29） Consistent with protein count
Chain P 11–284（274 aa）
Chain Q 11–284（274 aa）
Chain R 1–29（29 aa）
Chain S 1–29（29 aa）
Chain W 11–284（274 aa）
Chain X 11–284（274 aa）
Chain Y 1–29（29 aa）
Chain Z 1–29（29 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 15 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 6.60 Å
6KN8 Structure of human cardiac thin filament in the calcium bound state Deposited 2019-08-03 Assembly 1 Protein heterocomplex Heteromer；Protein × 29 PDB declaration: 29-meric（29） Consistent with protein count
Chain P 11–284（274 aa）
Chain Q 11–284（274 aa）
Chain R 1–29（29 aa）
Chain S 1–29（29 aa）
Chain W 11–284（274 aa）
Chain X 11–284（274 aa）
Chain Y 1–29（29 aa）
Chain Z 1–29（29 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 15 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.80 Å
6UT2 3D structure of the leiomodin/tropomyosin binding interface Deposited 2019-10-29 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain B 1–14（14 aa）
Chain C 1–14（14 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 0.081；Pressure 1
NMR sample composition 0.5 mM [U-13C; U-15N] leiomodin peptide, 1 mM tropomyosin peptide, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5 mM [U-13C; U-15N] tropomyosin peptide, 1 mM leiomodin peptide, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.3 mM [U-15N] leiomodin peptide, 0.6 mM tropomyosin peptide, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.3 mM [U-15N] tropomyosin peptide, 0.6 mM leiomodin peptide, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
6X5Z Bovine Cardiac Myosin in Complex with Chicken Skeletal Actin and Human Cardiac Tropomyosin in the Rigor State Deposited 2020-05-27 Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain O 1–284（284 aa）
Chain P 1–284（284 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE；Thin filaments were reconstituted by first mixing F-actin and tropomyosin to final concentrations of 10 uM actin and 7 uM tropomyosin. Just before applying 1.5 uL actin-tropomyosin to a freshly glow discharged holey-carbon grid, the surfactant octyl B-D-glucopyranoside was added to the protein solution to a concentration of 12 nM. The grid sample was manually blotted for 1 second and a 1.5 uL drop of 7.5 uM myosin-S1 sub-fragment was then applied to the blotted grid sample. The sample was immediately blotted for 4 seconds and plunge-frozen in liquid ethane.
Resolution 4.24 Å
7UTI ALTERNATIVE MODELING OF TROPOMYOSIN IN HUMAN CARDIAC THIN FILAMENT IN THE CALCIUM BOUND STATE Deposited 2022-04-27 Assembly 1 Protein heterocomplex Heteromer；Protein × 32 PDB declaration: 32-meric（32） Consistent with protein count
Chain W 1–284（284 aa）
Chain b 1–284（284 aa）
Chain e 1–284（284 aa）
Chain f 1–284（284 aa）
Chain g 1–284（284 aa）
Chain h 1–284（284 aa）
Chain i 1–284（284 aa）
Chain j 1–284（284 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) 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) ADP ADENOSINE-5'-DIPHOSPHATE × 16 MG MAGNESIUM ION × 16 CA CALCIUM ION × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.80 Å
7UTL ALTERNATIVE MODELING OF TROPOMYOSIN IN HUMAN CARDIAC THIN FILAMENT IN THE CALCIUM FREE STATE Deposited 2022-04-27 Assembly 1 Protein heterocomplex Heteromer；Protein × 34 PDB declaration: 34-meric（34） Consistent with protein count
Chain W 1–284（284 aa）
Chain Z 1–284（284 aa）
Chain a 1–284（284 aa）
Chain b 1–284（284 aa）
Chain g 1–284（284 aa）
Chain h 1–284（284 aa）
Chain i 1–284（284 aa）
Chain j 1–284（284 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 18 MG MAGNESIUM ION × 18 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 6.60 Å
8EFH Helical reconstruction of the human cardiac actin-tropomyosin-myosin complex in complex with ADP-Mg2+ Deposited 2022-09-08 Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain O 1–284（284 aa）
Chain P 1–284（284 aa）
Not recorded MG MAGNESIUM ION × 6 ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
8EFI Helical reconstruction of the human cardiac actin-tropomyosin-myosin complex in the rigor form Deposited 2022-09-08 Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain O 1–284（284 aa）
Chain P 1–284（284 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 5 ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
8ENC Helical reconstruction of the human cardiac actin-tropomyosin-myosin loop 4 7G mutant complex Deposited 2022-09-29 Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain O 1–284（284 aa）
Chain P 1–284（284 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 5 ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å
8ZB7 Human left ventricle ATM complex Deposited 2024-04-26 Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric（16） Consistent with protein count
Chain L 45–210（166 aa）
Chain N 45–210（166 aa）
Chain O 45–210（166 aa）
Chain P 45–210（166 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.19 Å
9ZBL Helical Reconstruction of the Human Cardiac F-Actin-Tropomyosin Complex Deposited 2025-11-20 Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric（10） Consistent with protein count
Chain M 1–284（284 aa）
Chain N 1–284（284 aa）
Chain O 1–284（284 aa）
Chain P 1–284（284 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE；Blotting was performed with a blot force of 3 and a blot time of 3 s.
Resolution 2.79 Å
9ZBP Helical Reconstruction of the Complex of Pseudo-Acetylated Human Cardiac Actin (K326/328Q) and Tropomyosin Deposited 2025-11-21 Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric（10） Consistent with protein count
Chain M 1–284（284 aa）
Chain N 1–284（284 aa）
Chain O 1–284（284 aa）
Chain P 1–284（284 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE；Blotting was performed with a blot force of 3 and a blot time of 3 s.
Resolution 3.12 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.