4ehq

Crystal Structure of Calmodulin Binding Domain of Orai1 in Complex with Ca2+/Calmodulin Displays a Unique Binding Mode

Method: X-RAY DIFFRACTION Dmax: 76.7 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Calmodulin

Rattus norvegicus

UniProt P62161

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–149 Not recorded Calcium release-activated calcium channel protein 1 × 1 (Q96D31) 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

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.

22 other PDB entries and 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CALM_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–148; UniProt 2–149

Calcium release-activated calcium channel protein 1

OrganismNot specified

UniProt Q96D31

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 69–88 Not recorded Calmodulin × 1 (P62161) 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

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CRCM1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain G; PDBConstruct 1–20; UniProt 69–88

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 4ehq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4ehq
Deposition date deposition_date2012-04-03
Structure title titleCrystal Structure of Calmodulin Binding Domain of Orai1 in Complex with Ca2+/Calmodulin Displays a Unique Binding Mode
Keywords keywords;calmodulin, Orai1, calcium dependent inactivation, EF hand, Calcium binding, calcium-dependent inactivation, Calmodulin binding domain of Orai1, none, cytosol, PROTEIN BINDING ;; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier22.63
Radius of gyration Rg (electron density) rg_electron21.97
Forward intensity I(0) i07190750.00
Molecular weight molecular_weight19230.0 kDa
Excluded volume excluded_volume23684 ų
Envelope volume envelope_volume31512 ų
Hydration-shell volume shell_volume13070 ų
Envelope diameter envelope_diameter77.0
Shell Rg shell_rg26.21
Envelope Rg envelope_rg21.52
Shape Rg shape_rg21.96
Total Rg total_rg22.61
Total atoms total_atoms1362
Residues n_residues165
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax76.7
Rg (real space) rg_real22.78
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real7.1910e+06
I(0) uncertainty (real space) i0_real_error1.0620e+05
Rg (reciprocal space) rg_reciprocal22.74
I(0) (reciprocal space) i0_reciprocal7191000.0000
Solution quality estimate total_estimate0.8042
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.6
Skewness Skewness skewness0.339
Kurtosis Kurtosis kurtosis-0.762
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha817400.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.609; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.627; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)