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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：P02602 New Search
2PDB entries
2Biological assembly
2chain/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
5H53 The structure of rabbit skeletal muscle actomyosin rigor complex at 5.2 angstrom. Deposited 2016-11-04 Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain C 41–192（152 aa） Fragment：UNP residues 41-192
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 5.20 Å
6YSY Skeletal Myosin bound to MPH-220, MgADP-VO4 Deposited 2020-04-23 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 1–192（192 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 1 VO4 VANADATE ION × 1 MG MAGNESIUM ION × 1 PJT (9~{S})-5-methyl-12-(4-morpholin-4-ylphenyl)-9-oxidanyl-4-thia-2,12-diazatricyclo[7.3.0.0^{3,7}]dodeca-1,3(7),5-trien-8-one × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；35% PEG600, 20mM DTT; 100mM HEPES pH 7.0; 5% DMSO
Resolution 3.25 Å R-free 0.232

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.