2f3y

Calmodulin/IQ domain complex

Method: X-RAY DIFFRACTION Dmax: 54.2 Å Quality: EXCELLENT

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

Calmodulin

Homo sapiens

UniProt P62158

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 1–148 Not recorded Voltage-dependent L-type calcium channel alpha-1C subunit × 1 (Q13933) CA CALCIUM ION × 4 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.3;298 K;32% PEG 4000, 50mM TRIS, 50 mM MgCl2, pH 8.3, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.45 Å R-free 0.219

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.

105 other PDB entries and 176 assemblies. Open the comparison page and filter oligomeric states

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

Voltage-dependent L-type calcium channel alpha-1C subunit

OrganismNot specified

UniProt Q13933

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 1665–1685 Not recorded Calmodulin × 1 (P62158) CA CALCIUM ION × 4 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.3;298 K;32% PEG 4000, 50mM TRIS, 50 mM MgCl2, pH 8.3, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.45 Å R-free 0.219

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.

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

View Construct and Data Evidence
UniProt name CAC1C_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–21; UniProt 1665–1685

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 2f3y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2f3y
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2f3y
Deposition date deposition_date2005-11-22
Structure title titleCalmodulin/IQ domain complex
Keywords keywordscalmodulin, calmodulin complex, calcium channnel, Cav1.2, IQ domain, METAL BINDING PROTEIN; METAL BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.36
Radius of gyration Rg (electron density) rg_electron15.98
Forward intensity I(0) i07255680.00
Molecular weight molecular_weight19108.0 kDa
Excluded volume excluded_volume23600 ų
Envelope volume envelope_volume27348 ų
Hydration-shell volume shell_volume14621 ų
Envelope diameter envelope_diameter53.3
Shell Rg shell_rg21.56
Envelope Rg envelope_rg16.13
Shape Rg shape_rg15.97
Total Rg total_rg16.94
Total atoms total_atoms1331
Residues n_residues164
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 dmax54.2
Rg (real space) rg_real17.28
Rg uncertainty (real space) rg_real_error0.29
I(0) (real space) i0_real7.2560e+06
I(0) uncertainty (real space) i0_real_error8.2610e+04
Rg (reciprocal space) rg_reciprocal17.29
I(0) (reciprocal space) i0_reciprocal7256000.0000
Solution quality estimate total_estimate0.9006
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.4
Skewness Skewness skewness0.182
Kurtosis Kurtosis kurtosis-0.405
Angular range angular_range— – 0.4600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha904700.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.906; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.990

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2f3ya_
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

CATH v4.4 (2 domains)

Domain ID domain_id2f3yA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id2f3yA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand

8. Citations (4)

9. Files and Curves (10)