6c0a

Actinin-1 EF-Hand bound to the Cav1.2 IQ Motif

Method: SOLUTION NMR Dmax: 47.3 Å Quality: GOOD

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

Alpha-actinin-1

Mus musculus

UniProt Q7TPR4

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 822–892 Fragment:EF-hand 3,4 (UNP residues 822-892) Voltage-dependent L-type calcium channel subunit alpha-1C × 1 (Q13936) SOLUTION NMR NMR measurement conditions:pH 7.5;303 K;Ionic strength (raw mmCIF value) 0;Pressure 1 NMR sample composition:300 uM [U-99% 15N] Actinin-1 EF hand, 300 uM IQ Motif, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:300 uM [U-99% 15N] Cav1.2 IQ Motif, 300 uM Actinin-1 EF 3,3, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:300 uM [U-99% 13C; U-99% 15N] Actinin-1 EF 3,4, 300 uM Cav1.2 IQ Motif, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:12 mg/mL Pf1 phage, 300 uM [U-99% 15N] Actinin-1 EF 3,4, 300 uM Cav1.2 IQ Motif, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:12 mg/mL Pf1 phage, 300 uM [U-99% 15N] Cav1.2 IQ Motif, 300 uM Actinin-1 EF 3,4, 90% H2O/10% D2O | 90% H2O/10% D2O Resolution not provided

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name ACTN1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–71; UniProt 822–892

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

OrganismNot specified

UniProt Q13936

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 1587–1609 Fragment:IQ Motif (UNP residues 1587-1609) Alpha-actinin-1 × 1 (Q7TPR4) SOLUTION NMR NMR measurement conditions:pH 7.5;303 K;Ionic strength (raw mmCIF value) 0;Pressure 1 NMR sample composition:300 uM [U-99% 15N] Actinin-1 EF hand, 300 uM IQ Motif, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:300 uM [U-99% 15N] Cav1.2 IQ Motif, 300 uM Actinin-1 EF 3,3, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:300 uM [U-99% 13C; U-99% 15N] Actinin-1 EF 3,4, 300 uM Cav1.2 IQ Motif, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:12 mg/mL Pf1 phage, 300 uM [U-99% 15N] Actinin-1 EF 3,4, 300 uM Cav1.2 IQ Motif, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:12 mg/mL Pf1 phage, 300 uM [U-99% 15N] Cav1.2 IQ Motif, 300 uM Actinin-1 EF 3,4, 90% H2O/10% D2O | 90% H2O/10% D2O Resolution not provided

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.

23 other PDB entries and 39 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CAC1C_HUMAN
Isoform Q13936-17
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–23; UniProt 1587–1609

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 6c0a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6c0a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6c0a
Deposition date deposition_date2017-12-28
Structure title titleActinin-1 EF-Hand bound to the Cav1.2 IQ Motif
Keywords keywords;actinin-1, EF hand, Calcium Calmodulin, Neuronal signaling, Voltage Gated Calcium Channel, Cav1.2, Voltage Gated Calcium Channel 1.2, Hippocampal Neurons, IQ Motif, SIGNALING PROTEIN ;; SIGNALING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier14.13
Radius of gyration Rg (electron density) rg_electron13.53
Forward intensity I(0) i028306200.00
Molecular weight molecular_weight43017.0 kDa
Excluded volume excluded_volume53781 ų
Envelope volume envelope_volume18457 ų
Hydration-shell volume shell_volume11530 ų
Envelope diameter envelope_diameter49.6
Shell Rg shell_rg19.38
Envelope Rg envelope_rg14.28
Shape Rg shape_rg13.53
Total Rg total_rg13.99
Total atoms total_atoms5952
Residues n_residues376
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 dmax47.3
Rg (real space) rg_real14.10
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real2.8310e+07
I(0) uncertainty (real space) i0_real_error3.4750e+05
Rg (reciprocal space) rg_reciprocal14.11
I(0) (reciprocal space) i0_reciprocal28310000.0000
Solution quality estimate total_estimate0.7731
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary17.4
Skewness Skewness skewness0.286
Kurtosis Kurtosis kurtosis-0.114
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha151700.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.682; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id6c0aA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand

8. Citations (2)

9. Files and Curves (10)