7sx3

Human NALCN-FAM155A-UNC79-UNC80 channelosome with CaM bound, conformation 1/2

Method: ELECTRON MICROSCOPY Dmax: 276.4 Å Quality: GOOD

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

Sodium leak channel non-selective protein,Enhanced green fluorescent protein

Homo sapiens

UniProt A0A7G8ZY66

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–241 Non-standard monomer:Yes (specific site not provided by mmCIF) Transmembrane protein FAM155A × 1 (B1AL88) Calmodulin-1 × 1 (P0DP23) UNC79,Protein unc-79 homolog,Protein unc-79 homolog × 1 (Q9P2D8) Protein unc-80 homolog × 1 (Q8N2C7) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 PEV (1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE × 4 PGV (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE × 2 Y01 CHOLESTEROL HEMISUCCINATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3.5 sec blotting Resolution 3.10 Å

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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A7G8ZY66_MUHV1
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1760–2000; UniProt 1–241

Sodium leak channel non-selective protein,Enhanced green fluorescent protein

Homo sapiens

UniProt Q8IZF0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–1738 Non-standard monomer:Yes (specific site not provided by mmCIF) Transmembrane protein FAM155A × 1 (B1AL88) Calmodulin-1 × 1 (P0DP23) UNC79,Protein unc-79 homolog,Protein unc-79 homolog × 1 (Q9P2D8) Protein unc-80 homolog × 1 (Q8N2C7) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 PEV (1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE × 4 PGV (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE × 2 Y01 CHOLESTEROL HEMISUCCINATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3.5 sec blotting Resolution 3.10 Å

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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NALCN_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1738; UniProt 1–1738

Transmembrane protein FAM155A

Homo sapiens

UniProt B1AL88

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 1–458 Not recorded Sodium leak channel non-selective protein,Enhanced green fluorescent protein × 1 (Q8IZF0,A0A7G8ZY66) Calmodulin-1 × 1 (P0DP23) UNC79,Protein unc-79 homolog,Protein unc-79 homolog × 1 (Q9P2D8) Protein unc-80 homolog × 1 (Q8N2C7) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 PEV (1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE × 4 PGV (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE × 2 Y01 CHOLESTEROL HEMISUCCINATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3.5 sec blotting Resolution 3.10 Å

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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name F155A_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–458; UniProt 1–458

Calmodulin-1

Homo sapiens

UniProt P0DP23

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 1–149 Not recorded Sodium leak channel non-selective protein,Enhanced green fluorescent protein × 1 (Q8IZF0,A0A7G8ZY66) Transmembrane protein FAM155A × 1 (B1AL88) UNC79,Protein unc-79 homolog,Protein unc-79 homolog × 1 (Q9P2D8) Protein unc-80 homolog × 1 (Q8N2C7) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 PEV (1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE × 4 PGV (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE × 2 Y01 CHOLESTEROL HEMISUCCINATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3.5 sec blotting Resolution 3.10 Å

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.

213 other PDB entries and 279 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CALM1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–149; UniProt 1–149

UNC79,Protein unc-79 homolog,Protein unc-79 homolog

Homo sapiens

UniProt Q9P2D8

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 174–2635 Not recorded Sodium leak channel non-selective protein,Enhanced green fluorescent protein × 1 (Q8IZF0,A0A7G8ZY66) Transmembrane protein FAM155A × 1 (B1AL88) Calmodulin-1 × 1 (P0DP23) Protein unc-80 homolog × 1 (Q8N2C7) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 PEV (1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE × 4 PGV (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE × 2 Y01 CHOLESTEROL HEMISUCCINATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3.5 sec blotting Resolution 3.10 Å

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 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UNC79_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 75–2536; UniProt 174–2635

Protein unc-80 homolog

Homo sapiens

UniProt Q8N2C7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 1–3258 Not recorded Sodium leak channel non-selective protein,Enhanced green fluorescent protein × 1 (Q8IZF0,A0A7G8ZY66) Transmembrane protein FAM155A × 1 (B1AL88) Calmodulin-1 × 1 (P0DP23) UNC79,Protein unc-79 homolog,Protein unc-79 homolog × 1 (Q9P2D8) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 PEV (1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE × 4 PGV (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE × 2 Y01 CHOLESTEROL HEMISUCCINATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3.5 sec blotting Resolution 3.10 Å

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 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UNC80_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–3258; UniProt 1–3258

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 7sx3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7sx3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7sx3
Deposition date deposition_date2021-11-22
Structure title titleHuman NALCN-FAM155A-UNC79-UNC80 channelosome with CaM bound, conformation 1/2
Keywords keywordsion channel, calmodulin, HEAT repeat protein, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier75.75
Radius of gyration Rg (electron density) rg_electron75.96
Forward intensity I(0) i03598070000.00
Molecular weight molecular_weight540120.0 kDa
Excluded volume excluded_volume689100 ų
Envelope volume envelope_volume1092900 ų
Hydration-shell volume shell_volume128370 ų
Envelope diameter envelope_diameter305.3
Shell Rg shell_rg68.09
Envelope Rg envelope_rg75.22
Shape Rg shape_rg75.98
Total Rg total_rg75.73
Total atoms total_atoms37959
Residues n_residues4681
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 dmax276.4
Rg (real space) rg_real80.29
Rg uncertainty (real space) rg_real_error2.04
I(0) (real space) i0_real3.6300e+09
I(0) uncertainty (real space) i0_real_error7.4620e+07
Rg (reciprocal space) rg_reciprocal74.25
I(0) (reciprocal space) i0_reciprocal3584000000.0000
Solution quality estimate total_estimate0.8743
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary79.0
Skewness Skewness skewness0.613
Kurtosis Kurtosis kurtosis0.029
Angular range angular_range— – 0.1050 −1
Current regularization parameter α current_alpha1.0780
Highest regularization parameter α highest_alpha199700000.0000
Real-space data points n_real_points22
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.830; Stabil: 0.838; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.425

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)