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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：Q13586 New Search
6PDB entries
12Biological assembly
22chain/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
2K60 NMR structure of calcium-loaded STIM1 EF-SAM Deposited 2008-07-02 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 58–201（144 aa） Fragment：UNP residues 58-201
Not recorded CA CALCIUM ION × 1 SOLUTION NMR
NMR measurement conditions pH 8；293 K；Ionic strength (raw mmCIF value) 105；Pressure 1
NMR measurement conditions 293 K；Ionic strength (raw mmCIF value) 105；Pressure 1
NMR sample composition 0.5-1.0 mM [U-100% 13C; U-100% 15N] stromal interaction molecule 1, 20 mM TRIS, 100 mM sodium chloride, 5 mM CALCIUM ION, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 0.5-1.0 mM [U-100% 13C; U-100% 15N] stromal interaction molecule 1, 20 mM [U-99% 2H] TRIS, 100 mM sodium chloride, 5 mM CALCIUM ION, 100% D2O | 100% D2O
Resolution not provided
2MAJ Solution Structure of the STIM1 CC1-CC2 homodimer. Deposited 2013-07-12 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 312–387（76 aa） Fragment：UNP residues 312-387
Chain C 312–387（76 aa） Fragment：UNP residues 312-387
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.5；308 K；Ionic strength (raw mmCIF value) 0.02；Pressure ambient
NMR sample composition 0.5 mM [U-99% 15N] protein, 20 mM bis-TRIS, 0.175 v/v [U-99% 2H] TFE, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5 mM [U-99% 13C; U-99% 15N] protein, 20 mM bis-TRIS, 0.175 v/v [U-99% 2H] TFE, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5 mM [U-99% 13C; U-99% 15N] protein, 20 mM bis-TRIS, 0.175 v/v [U-99% 2H] TFE, 100% D2O | 100% D2O
NMR sample composition 0.5 mM [U-99% 13C; U-99% 15N] protein, 0.5 mM protein, 20 mM bis-TRIS, 0.175 v/v [U-99% 2H] TFE, 100% D2O | 100% D2O
Resolution not provided
2MAK Solution structure of the STIM1 CC1-CC2 homodimer in complex with two Orai1 C-terminal domains. Deposited 2013-07-12 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 312–387（76 aa） Fragment：UNP residues 312-387
Chain C 312–387（76 aa） Fragment：UNP residues 312-387
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.5；308 K；Ionic strength (raw mmCIF value) 0.02；Pressure ambient
NMR sample composition 0.25 mM [U-100% 15N] protein_1, 3.0 mM protein_2, 20 mM bis-TRIS, 0.175 v/v [U-99% 2H] TFE, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.25 mM [U-99% 13C; U-99% 15N] protein_1, 3.0 mM protein_2, 20 mM bis-TRIS, 0.175 v/v [U-99% 2H] TFE, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.25 mM [U-99% 13C; U-99% 15N] protein_1, 3.0 mM protein_2, 20 mM bis-TRIS, 0.175 v/v [U-99% 2H] TFE, 100% D2O | 100% D2O
NMR sample composition 2.5 mM protein_1, 0.25 mM [U-99% 15N] protein_2, 20 mM bis-TRIS, 0.175 v/v [U-99% 2H] TFE, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 2.5 mM protein_1, 0.25 mM [U-99% 13C; U-99% 15N] protein_2, 20 mM bis-TRIS, 0.175 v/v [U-99% 2H] TFE, 100% D2O | 100% D2O
Resolution not provided
3TEQ Crystal structure of SOAR domain Deposited 2011-08-15 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 344–444（101 aa） Fragment：SOAR domain (UNP RESIDUES 344-444)
Chain C 344–444（101 aa） Fragment：SOAR domain (UNP RESIDUES 344-444)
Mutation：L374M, V419A, C437T Mutation：L374M, V419A, C437T PO4 PHOSPHATE ION × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；0.1M Bis-Tris pH 6.5, 10% PEG3350, 0.2M Ammonium dibasic phosphate, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 1.90 Å R-free 0.249
3TEQ Crystal structure of SOAR domain Deposited 2011-08-15 Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 344–444（101 aa） Fragment：SOAR domain (UNP RESIDUES 344-444)
Mutation：L374M, V419A, C437T No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；0.1M Bis-Tris pH 6.5, 10% PEG3350, 0.2M Ammonium dibasic phosphate, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 1.90 Å R-free 0.249
3TEQ Crystal structure of SOAR domain Deposited 2011-08-15 Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain D 344–444（101 aa） Fragment：SOAR domain (UNP RESIDUES 344-444)
Mutation：L374M, V419A, C437T No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；0.1M Bis-Tris pH 6.5, 10% PEG3350, 0.2M Ammonium dibasic phosphate, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 1.90 Å R-free 0.249
4O9B The Structure of CC1-IH in human STIM1. Deposited 2014-01-02 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 237–340（104 aa） Fragment：CC1-IH, UNP RESIDUES 237-340
Chain D 237–340（104 aa） Fragment：CC1-IH, UNP RESIDUES 237-340
Mutation：M244L, L321M Mutation：M244L, L321M CD CADMIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；293 K；24% PEGMME 2000, 0.1M sodium acetate, 0.02M magnesium chloride hexahydrate, 0.02M nickel chloride hexahydrate, 0.02M cadmium chloride hexahydrate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.60 Å R-free 0.289
4O9B The Structure of CC1-IH in human STIM1. Deposited 2014-01-02 Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 237–340（104 aa） Fragment：CC1-IH, UNP RESIDUES 237-340
Chain C 237–340（104 aa） Fragment：CC1-IH, UNP RESIDUES 237-340
Mutation：M244L, L321M Mutation：M244L, L321M CD CADMIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；293 K；24% PEGMME 2000, 0.1M sodium acetate, 0.02M magnesium chloride hexahydrate, 0.02M nickel chloride hexahydrate, 0.02M cadmium chloride hexahydrate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.60 Å R-free 0.289
4O9B The Structure of CC1-IH in human STIM1. Deposited 2014-01-02 Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 237–340（104 aa） Fragment：CC1-IH, UNP RESIDUES 237-340
Chain B 237–340（104 aa） Fragment：CC1-IH, UNP RESIDUES 237-340
Mutation：M244L, L321M Mutation：M244L, L321M CD CADMIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；293 K；24% PEGMME 2000, 0.1M sodium acetate, 0.02M magnesium chloride hexahydrate, 0.02M nickel chloride hexahydrate, 0.02M cadmium chloride hexahydrate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.60 Å R-free 0.289
4O9B The Structure of CC1-IH in human STIM1. Deposited 2014-01-02 Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain C 237–340（104 aa） Fragment：CC1-IH, UNP RESIDUES 237-340
Chain D 237–340（104 aa） Fragment：CC1-IH, UNP RESIDUES 237-340
Mutation：M244L, L321M Mutation：M244L, L321M CD CADMIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；293 K；24% PEGMME 2000, 0.1M sodium acetate, 0.02M magnesium chloride hexahydrate, 0.02M nickel chloride hexahydrate, 0.02M cadmium chloride hexahydrate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.60 Å R-free 0.289
4O9B The Structure of CC1-IH in human STIM1. Deposited 2014-01-02 Assembly 5 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 237–340（104 aa） Fragment：CC1-IH, UNP RESIDUES 237-340
Chain B 237–340（104 aa） Fragment：CC1-IH, UNP RESIDUES 237-340
Chain C 237–340（104 aa） Fragment：CC1-IH, UNP RESIDUES 237-340
Chain D 237–340（104 aa） Fragment：CC1-IH, UNP RESIDUES 237-340
Mutation：M244L, L321M Mutation：M244L, L321M Mutation：M244L, L321M Mutation：M244L, L321M CD CADMIUM ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；293 K；24% PEGMME 2000, 0.1M sodium acetate, 0.02M magnesium chloride hexahydrate, 0.02M nickel chloride hexahydrate, 0.02M cadmium chloride hexahydrate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.60 Å R-free 0.289
6YEL Stromal interaction molecule 1 coiled-coil 1 fragment Deposited 2020-03-25 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 234–343（110 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.25；310.15 K；Ionic strength (raw mmCIF value) 0.02；Pressure 1
NMR sample composition 0.3 mM [U-98% 13C; U-98% 15N] STIM1 CC1, 20 mM TRIS, 7 mM [U-13C] SDS, 90 % v/v H2O, 10 % v/v [U-99% 2H] H2O, 90% H2O/10% D2O | 90% H2O/10% 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.