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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：P04573 New Search
4PDB entries
4Biological assembly
4chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different experimental conditions

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
1C7V NMR SOLUTION STRUCTURE OF THE CALCIUM-BOUND C-TERMINAL DOMAIN (W81-S161) OF CALCIUM VECTOR PROTEIN FROM AMPHIOXUS Deposited 2000-03-27 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 81–161（81 aa） Fragment：C-TERMINAL DOMAIN (RESIDUES 81-161)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；308 K；Ionic strength (raw mmCIF value) 100 mM KCl；Pressure ambient
NMR sample composition Unlabeled | Deuterated Tris buffer (20 mM), 100 mM KCl, pH 6.5, 7% D2O
NMR sample composition Uniformly 15N labeled | Deuterated Tris buffer (20 mM), 100 mM KCl, pH 6.5
Resolution not provided
1C7W NMR SOLUTION STRUCTURE OF THE CALCIUM-BOUND C-TERMINAL DOMAIN (W81-S161) OF CALCIUM VECTOR PROTEIN FROM AMPHIOXUS Deposited 2000-03-27 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 81–161（81 aa） Fragment：C-TERMINAL DOMAIN (RESIDUES 81-161)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；308 K；Ionic strength (raw mmCIF value) 100 mM KCl；Pressure ambient
NMR sample composition Unlabeled | Deuterated Tris buffer (20 mM), 100 mM KCl, pH 6.5, 7% D2O
NMR sample composition Uniformly 15N labeled | Deuterated Tris buffer (20 mM), 100 mM KCl, pH 6.5
Resolution not provided
1J7Q Solution structure and backbone dynamics of the defunct EF-hand domain of Calcium Vector Protein Deposited 2001-05-18 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 1–86（86 aa） Fragment：N-terminal domain (residues 1-86)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 100 mM KCL；Pressure ambient
NMR sample composition 1.5 mM N-CaVP unlabeled, 20 mM Deuterated Tris buffer, 100 mM KCl | 8% D20
NMR sample composition 1.5 mM N-CaVP uniformly 15N labeled, 20 mM Deuterated Tris buffer, 100 mM KCl | 8% D20
Resolution not provided
1J7R Solution structure and backbone dynamics of the defunct EF-hand domain of Calcium Vector Protein Deposited 2001-05-18 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 1–86（86 aa） Fragment：N-terminal domain (residues 1-86)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 100 mM KCL；Pressure ambient
NMR sample composition 1.5 mM N-CaVP unlabeled, 20 mM Deuterated Tris buffer, 100 mM KCl | 8% D20
NMR sample composition 1.5 mM N-CaVP uniformly 15N labeled, 20 mM Deuterated Tris buffer, 100 mM KCl | 8% D20
Resolution not provided

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.