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6ctb

Apo-Calmodulin Bound to Calcium Voltage Gated Channel 1.2 IQ-Motif

Method: SOLUTION NMR Dmax: 46.7 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Calmodulin-1

Xenopus laevis

UniProt P0DP33

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 3–149 Not recorded Voltage-dependent L-type calcium channel subunit alpha-1C × 1 （P15381） SOLUTION NMR NMR measurement conditions：pH 6；303 K；Ionic strength (raw mmCIF value) 100；Pressure 1 NMR sample composition：300 uM [U-99% 15N] apo-Calmodulin, 300 uM Calcium Voltage Gated Channel 1.2, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition：300 uM [U-99% 15N] Calcium Voltage Gated Channel 1.2, 300 uM apo-Calmodulin, 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.

Other PDB Difference from Current Entry 6CTB Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1CKK CALMODULIN/RAT CA2+/CALMODULIN DEPENDENT PROTEIN KINASE FRAGMENT Deposited 1998-11-20 Different construct Different ligand/ion Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 2–149（148 aa）
Not recorded CA CALCIUM ION × 4 SOLUTION NMR
NMR measurement conditions pH 6.7；303 K；Ionic strength (raw mmCIF value) 100mM KCL, 10mM CACL2
Resolution not provided

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

View Construct and Data Evidence
UniProt name CALM1_XENLA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–147； UniProt 3–149

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

Oryctolagus cuniculus

UniProt P15381

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 1644–1668 Not recorded Calmodulin-1 × 1 （P0DP33） SOLUTION NMR NMR measurement conditions：pH 6；303 K；Ionic strength (raw mmCIF value) 100；Pressure 1 NMR sample composition：300 uM [U-99% 15N] apo-Calmodulin, 300 uM Calcium Voltage Gated Channel 1.2, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition：300 uM [U-99% 15N] Calcium Voltage Gated Channel 1.2, 300 uM apo-Calmodulin, 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.

Other PDB Difference from Current Entry 6CTB Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
4DEY Crystal structure of the Voltage Dependent Calcium Channel beta-2 Subunit in Complex With The CaV1.2 I-II Linker. Deposited 2012-01-22 Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 435–539（105 aa） Fragment：Intracellular I-II linker
Not recorded BR BROMIDE ION × 17 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；292 K；1.1-1.25 M potassium sodium tartrate, 0.1 M Tris Soaked with KI before freezing , pH 7.5, VAPOR DIFFUSION, temperature 292K
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；292 K；1.1-1.25 M potassium sodium tartrate, 0.1 M Tris Soaked with KI before freezing, pH 7.5, VAPOR DIFFUSION, temperature 292K
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；292 K；1.1-1.25 M potassium sodium tartrate, 0.1 M Tris Soaked with NaBr before freezing, pH 7.5, VAPOR DIFFUSION, temperature 292K
Resolution 1.95 Å R-free 0.229

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

View Construct and Data Evidence
UniProt name CAC1C_RABIT
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B； PDBConstruct 1–25； UniProt 1644–1668

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 6ctb

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6ctb
Deposition date deposition_date2018-03-22
Structure title titleApo-Calmodulin Bound to Calcium Voltage Gated Channel 1.2 IQ-Motif
Keywords keywordscalmodulin, surface expression, Cav1.2, apo-calmodulin, voltage gated channel, calcium, neuronal signaling, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier13.59 Å
Radius of gyration Rg (electron density) rg_electron12.79 Å
Forward intensity I(0) i030041800.00
Molecular weight molecular_weight43040.0 kDa
Excluded volume excluded_volume53310 ų
Envelope volume envelope_volume18544 ų
Hydration-shell volume shell_volume11829 ų
Envelope diameter envelope_diameter45.8 Å
Shell Rg shell_rg19.08 Å
Envelope Rg envelope_rg13.56 Å
Shape Rg shape_rg12.78 Å
Total Rg total_rg13.31 Å
Total atoms total_atoms5916
Residues n_residues368
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 dmax46.7 Å
Rg (real space) rg_real13.49 Å
Rg uncertainty (real space) rg_real_error0.34 Å
I(0) (real space) i0_real3.0040e+07
I(0) uncertainty (real space) i0_real_error3.1880e+05
Rg (reciprocal space) rg_reciprocal13.50 Å
I(0) (reciprocal space) i0_reciprocal30040000.0000
Solution quality estimate total_estimate0.8372
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.9 Å
Skewness Skewness skewness0.045
Kurtosis Kurtosis kurtosis-0.207
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha257600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.628; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.996
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd6ctba_
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
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8. Citations (1)

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9. Files and Curves (10)