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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：P11798 New Search
4PDB entries
4Biological assembly
17chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion 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
1HKX Crystal structure of calcium/calmodulin-dependent protein kinase Deposited 2003-03-12 Assembly 1 Protein homooligomer Homooligomer；Protein × 14 PDB declaration: tetradecameric（14） Consistent with protein count
Chain A 336–478（143 aa） Fragment：ASSOCIATION DOMAIN, RESIDUES 336-478
Chain B 336–478（143 aa） Fragment：ASSOCIATION DOMAIN, RESIDUES 336-478
Chain C 336–478（143 aa） Fragment：ASSOCIATION DOMAIN, RESIDUES 336-478
Chain D 336–478（143 aa） Fragment：ASSOCIATION DOMAIN, RESIDUES 336-478
Chain E 336–478（143 aa） Fragment：ASSOCIATION DOMAIN, RESIDUES 336-478
Chain F 336–478（143 aa） Fragment：ASSOCIATION DOMAIN, RESIDUES 336-478
Chain G 336–478（143 aa） Fragment：ASSOCIATION DOMAIN, RESIDUES 336-478
Chain H 336–478（143 aa） Fragment：ASSOCIATION DOMAIN, RESIDUES 336-478
Chain I 336–478（143 aa） Fragment：ASSOCIATION DOMAIN, RESIDUES 336-478
Chain J 336–478（143 aa） Fragment：ASSOCIATION DOMAIN, RESIDUES 336-478
Chain K 336–478（143 aa） Fragment：ASSOCIATION DOMAIN, RESIDUES 336-478
Chain L 336–478（143 aa） Fragment：ASSOCIATION DOMAIN, RESIDUES 336-478
Chain M 336–478（143 aa） Fragment：ASSOCIATION DOMAIN, RESIDUES 336-478
Chain N 336–478（143 aa） Fragment：ASSOCIATION DOMAIN, RESIDUES 336-478
Not recorded DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 1 CL CHLORIDE ION × 14 TBR HEXATANTALUM DODECABROMIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 4.8；pH 4.80
Resolution 2.65 Å R-free 0.279
7B55 Crystal structure of CaMKII-actinin complex bound to MES Deposited 2020-12-03 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 1–315（315 aa）
Not recorded MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.1 M MES pH 6.0, 20% w/v PEG4000, 0.2 M Lithium Sulfate
Resolution 1.60 Å R-free 0.214
7B56 Crystal structure of CaMKII-actinin complex bound to AMPPNP Deposited 2020-12-03 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 1–315（315 aa）
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.1 M MES pH 6.0, 20% w/v PEG4000, 0.2 M Lithium Sulfate
Resolution 1.45 Å R-free 0.215
7B57 Crystal structure of CaMKII-actinin complex bound to ADP Deposited 2020-12-03 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 1–315（315 aa）
Not recorded MG MAGNESIUM ION × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.1 M MES pH 6.0, 20% w/v PEG4000, 0.2 M Lithium Sulfate
Resolution 1.95 Å R-free 0.247

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.