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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：P12368 New Search
5PDB entries
7Biological assembly
24chain/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
2DRN Docking and dimerization domain (D/D) of the Type II-alpha regulatory subunity of protein kinase A (PKA) in complex with a peptide from an A-kinase anchoring protein Deposited 2006-06-11 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 2–44（43 aa） Fragment：N-terminal docking and dimerization domain, residues 4-46
Chain B 2–44（43 aa） Fragment：N-terminal docking and dimerization domain, residues 4-46
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 4；298 K；Pressure 1
NMR sample composition 2mM RII-alpha(1-44); 90% H2O, 10% D2O | 90% H2O/10% D2O
Resolution not provided
2H9R Docking and dimerization domain (D/D) of the regulatory subunit of the Type II-alpha cAMP-dependent protein kinase A associated with a Peptide derived from an A-kinase anchoring protein (AKAP) Deposited 2006-06-10 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 2–44（43 aa） Fragment：N-terminal docking and dimerization domain, residues 4-46
Chain B 2–44（43 aa） Fragment：N-terminal docking and dimerization domain, residues 4-46
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 4；298 K；Pressure 1
NMR sample composition 2mM RII-alpha(1-44); 90% H2O, 10% D2O | 90% H2O/10% D2O
Resolution not provided
2HWN Crystal Structure of RII alpha Dimerization/Docking domain of PKA bound to the D-AKAP2 peptide Deposited 2006-08-01 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 0–44（45 aa） Fragment：Dimerization/docking domain, residues 0-44
Chain B 0–44（45 aa） Fragment：Dimerization/docking domain, residues 0-44
Not recorded GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；100mM HEPES, 20% PEG 8000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.60 Å R-free 0.239
2HWN Crystal Structure of RII alpha Dimerization/Docking domain of PKA bound to the D-AKAP2 peptide Deposited 2006-08-01 Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain C 0–44（45 aa） Fragment：Dimerization/docking domain, residues 0-44
Chain D 0–44（45 aa） Fragment：Dimerization/docking domain, residues 0-44
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；100mM HEPES, 20% PEG 8000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.60 Å R-free 0.239
2HWN Crystal Structure of RII alpha Dimerization/Docking domain of PKA bound to the D-AKAP2 peptide Deposited 2006-08-01 Assembly 3 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain A 0–44（45 aa） Fragment：Dimerization/docking domain, residues 0-44
Chain B 0–44（45 aa） Fragment：Dimerization/docking domain, residues 0-44
Chain C 0–44（45 aa） Fragment：Dimerization/docking domain, residues 0-44
Chain D 0–44（45 aa） Fragment：Dimerization/docking domain, residues 0-44
Not recorded GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；100mM HEPES, 20% PEG 8000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.60 Å R-free 0.239
2IZY Molecular Basis of AKAP Specificity for PKA Regulatory Subunits Deposited 2006-07-27 Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric（8） Consistent with protein count
Chain A 2–44（43 aa） Fragment：RESIDUES 2-44
Chain B 2–44（43 aa） Fragment：RESIDUES 2-44
Chain C 2–44（43 aa） Fragment：RESIDUES 2-44
Chain D 2–44（43 aa） Fragment：RESIDUES 2-44
Chain E 2–44（43 aa） Fragment：RESIDUES 2-44
Chain F 2–44（43 aa） Fragment：RESIDUES 2-44
Chain G 2–44（43 aa） Fragment：RESIDUES 2-44
Chain H 2–44（43 aa） Fragment：RESIDUES 2-44
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.8；8-10% PEG400, 0.2-0.4 M SODIUM PHOSPHATE AND SODIUM CITRATE (PH 5.8)
Resolution 2.20 Å R-free 0.272
3TMH Crystal structure of dual-specific A-kinase anchoring protein 2 in complex with cAMP-dependent protein kinase A type II alpha and PDZK1 Deposited 2011-08-31 Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric（20） Consistent with protein count
Chain B 1–45（45 aa） Fragment：Dimerization/docking domain (D/D), UNP RESIDUES 3-44
Chain C 1–45（45 aa） Fragment：Dimerization/docking domain (D/D), UNP RESIDUES 3-44
Chain F 1–45（45 aa） Fragment：Dimerization/docking domain (D/D), UNP RESIDUES 3-44
Chain G 1–45（45 aa） Fragment：Dimerization/docking domain (D/D), UNP RESIDUES 3-44
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；pH 7；293 K；100 mM HEPES, pH 7, 20% PEG MME, Microbatch, temperature 293K
Resolution 3.80 Å R-free 0.328

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.