7bym

Cryo-EM structure of human KCNQ4 with retigabine

Method: ELECTRON MICROSCOPY Dmax: 134.9 Å Quality: GOOD

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

Green fluorescent protein,Potassium voltage-gated channel subfamily KQT member 4

Homo sapiens

UniProt P42212

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 2–238 Chain C; UniProt 2–238 Chain E; UniProt 2–238 Chain G; UniProt 2–238 Mutation:F64L/S65T/K107T/A206K/H231L Calmodulin-3 × 4 (P0DP25) PT5 [(2R)-1-octadecanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phospho ryl]oxy-propan-2-yl] (8Z)-icosa-5,8,11,14-tetraenoate × 4 FBX ethyl N-[2-azanyl-4-[(4-fluorophenyl)methylamino]phenyl]carbamate × 4 K POTASSIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE 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.

568 other PDB entries and 744 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 31–267; UniProt 2–238 Author chain C; PDBConstruct 31–267; UniProt 2–238 Author chain E; PDBConstruct 31–267; UniProt 2–238 Author chain G; PDBConstruct 31–267; UniProt 2–238

Green fluorescent protein,Potassium voltage-gated channel subfamily KQT member 4

Homo sapiens

UniProt P56696

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–695 Chain C; UniProt 1–695 Chain E; UniProt 1–695 Chain G; UniProt 1–695 Mutation:F64L/S65T/K107T/A206K/H231L Calmodulin-3 × 4 (P0DP25) PT5 [(2R)-1-octadecanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phospho ryl]oxy-propan-2-yl] (8Z)-icosa-5,8,11,14-tetraenoate × 4 FBX ethyl N-[2-azanyl-4-[(4-fluorophenyl)methylamino]phenyl]carbamate × 4 K POTASSIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE 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.

12 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KCNQ4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 285–979; UniProt 1–695 Author chain C; PDBConstruct 285–979; UniProt 1–695 Author chain E; PDBConstruct 285–979; UniProt 1–695 Author chain G; PDBConstruct 285–979; UniProt 1–695

Calmodulin-3

Homo sapiens

UniProt P0DP25

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 1–149 Chain D; UniProt 1–149 Chain F; UniProt 1–149 Chain H; UniProt 1–149 Not recorded Green fluorescent protein,Potassium voltage-gated channel subfamily KQT member 4 × 4 (P42212,P56696) PT5 [(2R)-1-octadecanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phospho ryl]oxy-propan-2-yl] (8Z)-icosa-5,8,11,14-tetraenoate × 4 FBX ethyl N-[2-azanyl-4-[(4-fluorophenyl)methylamino]phenyl]carbamate × 4 K POTASSIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE 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.

22 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CALM3_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–149; UniProt 1–149 Author chain D; PDBConstruct 1–149; UniProt 1–149 Author chain F; PDBConstruct 1–149; UniProt 1–149 Author chain H; PDBConstruct 1–149; UniProt 1–149

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 7bym

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7bym
Deposition date deposition_date2020-04-23
Structure title titleCryo-EM structure of human KCNQ4 with retigabine
Keywords keywordsKCNQ, Channel, Calmodulin, PIP2, retigabine, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.62
Radius of gyration Rg (electron density) rg_electron43.69
Forward intensity I(0) i0754498000.00
Molecular weight molecular_weight233170.0 kDa
Excluded volume excluded_volume294360 ų
Envelope volume envelope_volume430060 ų
Hydration-shell volume shell_volume79477 ų
Envelope diameter envelope_diameter137.8
Shell Rg shell_rg51.22
Envelope Rg envelope_rg42.49
Shape Rg shape_rg43.67
Total Rg total_rg44.10
Total atoms total_atoms16407
Residues n_residues2000
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 dmax134.9
Rg (real space) rg_real44.25
Rg uncertainty (real space) rg_real_error0.92
I(0) (real space) i0_real7.5450e+08
I(0) uncertainty (real space) i0_real_error1.3520e+07
Rg (reciprocal space) rg_reciprocal44.62
I(0) (reciprocal space) i0_reciprocal754800000.0000
Solution quality estimate total_estimate0.8922
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary57.8
Skewness Skewness skewness-0.039
Kurtosis Kurtosis kurtosis-0.525
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha42180000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.896; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.953; Smooth: 0.952

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id7bymB01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id7bymD01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id7bymF01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id7bymH01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand

8. Citations (1)

9. Files and Curves (10)