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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：P04775 New Search
3PDB entries
3Biological assembly
3chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion 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
1BYY SODIUM CHANNEL IIA INACTIVATION GATE Deposited 1998-10-21 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 1474–1526（53 aa） Fragment：INACTIVATION DOMAIN FRAGMENT
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；299 K
NMR sample composition H2O/D2O
Resolution not provided
2KXW Structure of the C-domain Fragment of apo Calmodulin Bound to the IQ motif of Nav1.2 Deposited 2010-05-13 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 1901–1927（27 aa） Fragment：IQ-motif of the Voltage-dependent Sodium Channel (UNP Residues 1901-1927)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 100；Pressure ambient
NMR sample composition 1.5 mM [U-100% 13C; U-100% 15N] C-domain of apo Calmodulin, 1.5 mM Voltage-dependent Sodium Channel v 1.2, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 1.5 mM Voltage-dependent Sodium Channel v 1.2, 1.5 mM [U-100% 13C; U-100% 15N] C-domain of apo Calmodulin, 100% D2O | 100% D2O
Resolution not provided
2M5E Structure of the C-domain of Calcium-saturated Calmodulin bound to the IQ motif of NaV1.2 Deposited 2013-02-21 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 1901–1927（27 aa） Fragment：UNP residues 1901-1927
Not recorded CA CALCIUM ION × 2 SOLUTION NMR
NMR measurement conditions pH 6.8；298 K；Pressure ambient
NMR sample composition 1.5 mM [U-100% 13C; U-100% 15N] C-domain of Calmodulin, 1.5 mM IQ motif peptide of NaV1.2, 3.3 mM CALCIUM ION, 10 mM [U-2H] imidazole, 100 mM potassium chloride, 0.01 % sodium azide, 50 uM [U-2H] EDTA, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 1.5 mM [U-100% 13C; U-100% 15N] C-domain of Calmodulin, 1.5 mM IQ motif peptide of NaV1.2, 3.3 mM CALCIUM ION, 10 mM [U-2H] imidazole, 100 mM potassium chloride, 0.01 % sodium azide, 50 uM [U-2H] EDTA, 100% D2O | 100% D2O
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.