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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：Q96D31 New Search
2PDB entries
2Biological assembly
3chain/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
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 B 272–292（21 aa） Fragment：Orai1 C-terminal domain, UNP residues 272-292
Chain D 272–292（21 aa） Fragment：Orai1 C-terminal domain, UNP residues 272-292
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
4EHQ Crystal Structure of Calmodulin Binding Domain of Orai1 in Complex with Ca2+/Calmodulin Displays a Unique Binding Mode Deposited 2012-04-03 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain G 69–88（20 aa）
Not recorded CA CALCIUM ION × 4 GBL GAMMA-BUTYROLACTONE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；0.1 M Bis-Tris pH 6.0, 40% PPG P400, 14% butyrolactone, 1% n-octyl-beta-D-glucopyranoside, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.90 Å R-free 0.216

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.