Current Protein Identity:Q99250 New Search
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
2KAV Solution structure of the human Voltage-gated Sodium Channel, brain isoform (Nav1.2) Deposited 2008-11-15 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1777–1882(106 aa) Fragment:C-terminal EF-Hand Domain
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.4;290.5 K;Ionic strength (raw mmCIF value) 0.1;Pressure ambient
NMR sample composition 0.5 mM [U-99% 13C; U-99% 15N] protein, 100 mM [D5-98%] glycine, 20 mM [D11-98 %] TRIS, 0.1 mM [D16-98%] EDTA, 10 % [U-99% 2H] D2O, 1 mM [D10-98%] DTT, 0.02 % NaN3, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5 mM [U-10% 13C; U-99% 15N] protein, 100 mM [D5-98%] glycine, 20 mM [D11-98 %] TRIS, 0.1 mM [D16-98%] EDTA, 10 % [U-99% 2H] D2O, 1 mM [D10-98%] DTT, 0.02 % NaN3, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5 mM [U-99% 13C; U-99% 15N] protein, 100 mM [D5-98%] glycine, 20 mM [D11-98 %] TRIS, 0.1 mM [D16-98%] EDTA, 10 % [U-99% 2H] D2O, 1 mM [D10-98%] DTT, 0.02 % NaN3, 15 mg pF1 phage, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
4JPZ Voltage-gated sodium channel 1.2 C-terminal domain in complex with FGF13U and Ca2+/calmodulin Deposited 2013-03-19 Assembly 1 Protein heterocomplex Heteromer;Protein × 3 PDB declaration: trimeric(3) Consistent with protein count
Chain B 1777–1937(161 aa)
Not recorded CA CALCIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION;pH 7.5;290 K;14% pEG3350, 300 mM sodium acetate,50 mM Tris pH 7.5, and 2 mM CaCl2, EVAPORATION, temperature 290K
Resolution 3.02 Å R-free 0.246
4JPZ Voltage-gated sodium channel 1.2 C-terminal domain in complex with FGF13U and Ca2+/calmodulin Deposited 2013-03-19 Assembly 2 Protein heterocomplex Heteromer;Protein × 3 PDB declaration: trimeric(3) Consistent with protein count
Chain H 1777–1937(161 aa)
Not recorded CA CALCIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION;pH 7.5;290 K;14% pEG3350, 300 mM sodium acetate,50 mM Tris pH 7.5, and 2 mM CaCl2, EVAPORATION, temperature 290K
Resolution 3.02 Å R-free 0.246
6BUT Solution structure of full-length apo mammalian calmodulin bound to the IQ motif of the human voltage-gated sodium channel NaV1.2 Deposited 2017-12-11 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 1901–1927(27 aa)
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 1
NMR measurement conditions pH 6.5;298 K;Ionic strength (raw mmCIF value) 100;Pressure 1
NMR sample composition 0.950 mM U-99% C13, U-99% N15 Calmodulin, 0.950 mM U-99% C13, U-99% N15 voltage-gated sodium channel NaV1.2 IQ motif, 0.1 mM U-98% 2H EDTA, 100 mM KCl, 10 mM [U-99% 2H] imidazole, 0.01 % w/v sodium azide, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.95 mM U-99% C13, U-99% N15 Calmodulin, 0.95 mM U-99% C13, U-99% N15 voltage-gated sodium channel NaV1.2 IQ motif, 0.1 mM U-98% 2H EDTA, 100 mM potassium chloride, 10 mM [U-99% 2H] imidazole, 0.01 % w/v sodium azide, 100% D2O | 100% D2O
Resolution not provided
6J8E Human Nav1.2-beta2-KIIIA ternary complex Deposited 2019-01-18 Assembly 1 Other combination Heteromer;Protein × 3 PDB declaration: trimeric(3) Consistent with protein count
Chain A 1–2005(2005 aa)
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 9Z9 (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en × 1 NA SODIUM ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 5.9
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 Å