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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：P11275 New Search
6PDB entries
7Biological assembly
42chain/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
1CDM MODULATION OF CALMODULIN PLASTICITY IN MOLECULAR RECOGNITION ON THE BASIS OF X-RAY STRUCTURES Deposited 1993-10-08 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 290–314（25 aa）
Not recorded CA CALCIUM ION × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å
1CM1 MOTIONS OF CALMODULIN-SINGLE-CONFORMER REFINEMENT Deposited 1997-09-23 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 290–314（25 aa） Fragment：CALMODULIN BINDING DOMAIN, RESIDUES 290 - 314
Not recorded CA CALCIUM ION × 5 X-RAY DIFFRACTION
X-ray crystallization conditions vapor diffusion - hanging drop - microseeding；pH 5.2；DIFFRACTION-QUALITY CRYSTALS WERE MICROSEEDED IN HANGING DROPS OVER 100 MM SODIUM ACETATE AT PH 5.2, WITH 20% POLY-ETHYLENE GLYCOL 6000 (PEG 6000), 10 MM CALCIUM CHLORIDE AND 0.02% SODIUM AZIDE. STOCK SOLUTIONS OF 24 MG/ML BOVINE BRAIN CALMODULIN (SIGMA LOT 54H9558), 14 MG/ML CAMKII-ALPHA PEPTIDE, AND 30% PEG WERE MIXED INTO HANGING DROPS IN ABOUT A 4-2-1 RATIO., vapor diffusion - hanging drop - microseeding
Resolution 2.00 Å R-free 0.302
1CM1 MOTIONS OF CALMODULIN-SINGLE-CONFORMER REFINEMENT Deposited 1997-09-23 Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain B 290–314（25 aa） Fragment：CALMODULIN BINDING DOMAIN, RESIDUES 290 - 314
Not recorded CA CALCIUM ION × 10 X-RAY DIFFRACTION
X-ray crystallization conditions vapor diffusion - hanging drop - microseeding；pH 5.2；DIFFRACTION-QUALITY CRYSTALS WERE MICROSEEDED IN HANGING DROPS OVER 100 MM SODIUM ACETATE AT PH 5.2, WITH 20% POLY-ETHYLENE GLYCOL 6000 (PEG 6000), 10 MM CALCIUM CHLORIDE AND 0.02% SODIUM AZIDE. STOCK SOLUTIONS OF 24 MG/ML BOVINE BRAIN CALMODULIN (SIGMA LOT 54H9558), 14 MG/ML CAMKII-ALPHA PEPTIDE, AND 30% PEG WERE MIXED INTO HANGING DROPS IN ABOUT A 4-2-1 RATIO., vapor diffusion - hanging drop - microseeding
Resolution 2.00 Å R-free 0.302
1CM4 Motions of calmodulin-four-conformer refinement Deposited 1997-09-23 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 290–314（25 aa） Fragment：CALMODULIN BINDING DOMAIN, RESIDUES 290 - 314
Not recorded CA CALCIUM ION × 17 X-RAY DIFFRACTION
X-ray crystallization conditions vapor diffusion - hanging drop - microseeding；pH 5.2；DIFFRACTION-QUALITY CRYSTALS WERE MICROSEEDED IN HANGING DROPS OVER 100 MM SODIUM ACETATE AT PH 5.2, WITH 20% POLY-ETHYLENE GLYCOL 6000 (PEG 6000), 10 MM CALCIUM CHLORIDE AND 0.02% SODIUM AZIDE. STOCK SOLUTIONS OF 24 MG/ML BOVINE BRAIN CALMODULIN (SIGMA LOT 54H9558), 14 MG/ML CAMKII-ALPHA PEPTIDE, AND 30% PEG WERE MIXED INTO HANGING DROPS IN ABOUT A 4-2-1 RATIO., vapor diffusion - hanging drop - microseeding
Resolution 2.00 Å R-free 0.262
5U6Y Pseudo-atomic model of the CaMKIIa holoenzyme. Deposited 2016-12-09 Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric（12） Consistent with protein count
Chain A 13–472（460 aa）
Chain B 13–472（460 aa）
Chain C 13–472（460 aa）
Chain D 13–472（460 aa）
Chain E 13–472（460 aa）
Chain F 13–472（460 aa）
Chain G 13–472（460 aa）
Chain H 13–472（460 aa）
Chain I 13–472（460 aa）
Chain J 13–472（460 aa）
Chain K 13–472（460 aa）
Chain L 13–472（460 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
Resolution 20.00 Å
8SYG Cryo-EM structure of tetradecameric hub domain of CaMKII alpha Deposited 2023-05-25 Assembly 1 Insufficient information Homooligomer；Protein × 14 PDB declaration: tetradecameric（14） Consistent with protein count
Chain A 345–478（134 aa）
Chain B 345–478（134 aa）
Chain C 345–478（134 aa）
Chain D 345–478（134 aa）
Chain E 345–478（134 aa）
Chain F 345–478（134 aa）
Chain G 345–478（134 aa）
Chain H 345–478（134 aa）
Chain I 345–478（134 aa）
Chain J 345–478（134 aa）
Chain K 345–478（134 aa）
Chain L 345–478（134 aa）
Chain M 345–478（134 aa）
Chain N 345–478（134 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.60 Å
8T15 Cryo-EM structure of dodecameric hub domain of CaMKII alpha Deposited 2023-06-01 Assembly 1 Insufficient information Homooligomer；Protein × 12 PDB declaration: dodecameric（12） Consistent with protein count
Chain A 345–478（134 aa）
Chain B 345–478（134 aa）
Chain C 345–478（134 aa）
Chain D 345–478（134 aa）
Chain E 345–478（134 aa）
Chain F 345–478（134 aa）
Chain G 345–478（134 aa）
Chain H 345–478（134 aa）
Chain I 345–478（134 aa）
Chain J 345–478（134 aa）
Chain K 345–478（134 aa）
Chain L 345–478（134 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.70 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.