3bxl

Crystal structure of the R-type calcium channeL (CaV2.3) IQ domain and CA2+calmodulin complex

Method: X-RAY DIFFRACTION Dmax: 52.9 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 Voltage-dependent R-type calcium channel subunit alpha-1E peptide × 1 (Q07652) CA CALCIUM ION × 4 SO4 SULFATE ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.30 Å R-free 0.262
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 2–149 Not recorded Voltage-dependent R-type calcium channel subunit alpha-1E peptide × 2 (Q07652) CA CALCIUM ION × 8 SO4 SULFATE ION × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.30 Å R-free 0.262

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 46 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

Voltage-dependent R-type calcium channel subunit alpha-1E peptide

OrganismNot specified

UniProt Q07652

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 B; UniProt 1819–1839 Not recorded Calmodulin × 1 (P62161) CA CALCIUM ION × 4 SO4 SULFATE ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.30 Å R-free 0.262
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1819–1839 Not recorded Calmodulin × 2 (P62161) CA CALCIUM ION × 8 SO4 SULFATE ION × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.30 Å R-free 0.262

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 CAC1E_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–21; UniProt 1819–1839

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 3bxl

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3bxl
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id3bxl
Deposition date deposition_date2008-01-14
Structure title titleCrystal structure of the R-type calcium channeL (CaV2.3) IQ domain and CA2+calmodulin complex
Keywords keywords;ION CHANNEL, CALMODULIN, CALCIUM CHANNEL, IQ DOMAIN, FACILLITATION, INACTIVATION, CALCIUM-DEPENDENT, VOLTAGE-GATED, ROBETTA, SIMULATIONS, Acetylation, Methylation, Phosphoprotein, Ubl conjugation, Calcium transport, Glycoprotein, Ion transport, Ionic channel, Membrane, Transmembrane, Transport, Voltage-gated channel, MEMBRANE PROTEIN, SIGNALING PROTEIN ;; MEMBRANE PROTEIN, SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.92
Radius of gyration Rg (electron density) rg_electron15.50
Forward intensity I(0) i07351020.00
Molecular weight molecular_weight18637.0 kDa
Excluded volume excluded_volume22795 ų
Envelope volume envelope_volume26298 ų
Hydration-shell volume shell_volume14404 ų
Envelope diameter envelope_diameter52.4
Shell Rg shell_rg21.26
Envelope Rg envelope_rg15.67
Shape Rg shape_rg15.52
Total Rg total_rg16.46
Total atoms total_atoms1291
Residues n_residues162
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 dmax52.9
Rg (real space) rg_real16.82
Rg uncertainty (real space) rg_real_error0.20
I(0) (real space) i0_real7.3510e+06
I(0) uncertainty (real space) i0_real_error7.8760e+04
Rg (reciprocal space) rg_reciprocal16.83
I(0) (reciprocal space) i0_reciprocal7351000.0000
Solution quality estimate total_estimate0.8993
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.6
Skewness Skewness skewness0.146
Kurtosis Kurtosis kurtosis-0.407
Angular range angular_range— – 0.4700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1091000.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.904; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.981

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3bxla_
Class classa — All alpha proteins
Fold Fold folda.39 — EF Hand-like
Superfamily Superfamily superfamilya.39.1 — EF-hand
Family Family familya.39.1.5 — Calmodulin-like

8. Citations (1)

9. Files and Curves (10)