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4o9b

The Structure of CC1-IH in human STIM1.

Method: X-RAY DIFFRACTION Dmax: 135.4 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Stromal interaction molecule 1

Homo sapiens

UniProt Q13586

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 237–340 Chain D； UniProt 237–340 Fragment：CC1-IH, UNP RESIDUES 237-340 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
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain B； UniProt 237–340 Chain C； UniProt 237–340 Fragment：CC1-IH, UNP RESIDUES 237-340 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
3 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 237–340 Chain B； UniProt 237–340 Fragment：CC1-IH, UNP RESIDUES 237-340 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
4 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain C； UniProt 237–340 Chain D； UniProt 237–340 Fragment：CC1-IH, UNP RESIDUES 237-340 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
5 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain A； UniProt 237–340 Chain B； UniProt 237–340 Chain C； UniProt 237–340 Chain D； UniProt 237–340 Fragment：CC1-IH, UNP RESIDUES 237-340 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

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 4O9B Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2K60 NMR structure of calcium-loaded STIM1 EF-SAM Deposited 2008-07-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
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 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
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 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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
6YEL Stromal interaction molecule 1 coiled-coil 1 fragment Deposited 2020-03-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
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

5 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name STIM1_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–104； UniProt 237–340 Author chain B； PDBConstruct 1–104； UniProt 237–340 Author chain C； PDBConstruct 1–104； UniProt 237–340 Author chain D； PDBConstruct 1–104； UniProt 237–340

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 4o9b

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4o9b
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4o9b
Deposition date deposition_date2014-01-02
Structure title titleThe Structure of CC1-IH in human STIM1.
Keywords keywords;SIGNALING PROTEIN, Structural Genomics, NPPSFA, National Project on Protein Structural and Functional Analyses, ALPHA HELICES, Signaling ;; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier51.10 Å
Radius of gyration Rg (electron density) rg_electron52.98 Å
Forward intensity I(0) i030730500.00
Molecular weight molecular_weight40932.0 kDa
Excluded volume excluded_volume49882 ų
Envelope volume envelope_volume96237 ų
Hydration-shell volume shell_volume19883 ų
Envelope diameter envelope_diameter218.6 Å
Shell Rg shell_rg40.32 Å
Envelope Rg envelope_rg54.10 Å
Shape Rg shape_rg53.03 Å
Total Rg total_rg52.06 Å
Total atoms total_atoms2858
Residues n_residues360
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax135.4 Å
Rg (real space) rg_real46.22 Å
Rg uncertainty (real space) rg_real_error0.56 Å
I(0) (real space) i0_real2.9220e+07
I(0) uncertainty (real space) i0_real_error4.7690e+05
Rg (reciprocal space) rg_reciprocal50.32 Å
I(0) (reciprocal space) i0_reciprocal30660000.0000
Solution quality estimate total_estimate0.6586
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.0 Å
Skewness Skewness skewness0.350
Kurtosis Kurtosis kurtosis-0.604
Angular range angular_range— – 0.1550 Å−1
Current regularization parameter α current_alpha0.5978
Highest regularization parameter α highest_alpha2189000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.010; Oscil: 0.919; Stabil: 0.972; Sysdev: 0.000; Positv: 1.000; Valcen: 0.896; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id4o9bA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily340 —
Domain ID domain_id4o9bB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily340 —
Domain ID domain_id4o9bC00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily340 —
Domain ID domain_id4o9bD00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily340 —
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8. Citations (1)

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9. Files and Curves (10)