9zwn

High-resolution cryo-EM structure of KdpFABC in the E2P state in lipid nanodisc

Method: ELECTRON MICROSCOPY Dmax: 152.2 Å Quality: GOOD

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

Potassium-transporting ATPase potassium-binding subunit

Escherichia coli

UniProt P03959

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–557 Not recorded Potassium-transporting ATPase ATP-binding subunit × 1 (P03960) Potassium-transporting ATPase KdpC subunit × 1 (P03961) Potassium-transporting ATPase KdpF subunit × 1 (P36937) K POTASSIUM ION × 3 9Y0 (2R)-3-(((2-aminoethoxy)(hydroxy)phosphoryl)oxy)-2-(palmitoyloxy)propyl (E)-octadec-9-enoate × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;20 mM Tris pH 7.4, 100 mM KCl, and 0.5 mM TCEP, 2 mM MgCl2, 1 mM ATP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.58 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 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KDPA_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–557; UniProt 1–557

Potassium-transporting ATPase ATP-binding subunit

Escherichia coli

UniProt P03960

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–682 Non-standard monomer:Yes (specific site not provided by mmCIF) Potassium-transporting ATPase potassium-binding subunit × 1 (P03959) Potassium-transporting ATPase KdpC subunit × 1 (P03961) Potassium-transporting ATPase KdpF subunit × 1 (P36937) K POTASSIUM ION × 3 9Y0 (2R)-3-(((2-aminoethoxy)(hydroxy)phosphoryl)oxy)-2-(palmitoyloxy)propyl (E)-octadec-9-enoate × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;20 mM Tris pH 7.4, 100 mM KCl, and 0.5 mM TCEP, 2 mM MgCl2, 1 mM ATP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.58 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.

26 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KDPB_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–682; UniProt 1–682

Potassium-transporting ATPase KdpC subunit

Escherichia coli

UniProt P03961

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–190 Not recorded Potassium-transporting ATPase potassium-binding subunit × 1 (P03959) Potassium-transporting ATPase ATP-binding subunit × 1 (P03960) Potassium-transporting ATPase KdpF subunit × 1 (P36937) K POTASSIUM ION × 3 9Y0 (2R)-3-(((2-aminoethoxy)(hydroxy)phosphoryl)oxy)-2-(palmitoyloxy)propyl (E)-octadec-9-enoate × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;20 mM Tris pH 7.4, 100 mM KCl, and 0.5 mM TCEP, 2 mM MgCl2, 1 mM ATP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.58 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.

21 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KDPC_ECOLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–190; UniProt 1–190

Potassium-transporting ATPase KdpF subunit

Escherichia coli

UniProt P36937

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 1–29 Not recorded Potassium-transporting ATPase potassium-binding subunit × 1 (P03959) Potassium-transporting ATPase ATP-binding subunit × 1 (P03960) Potassium-transporting ATPase KdpC subunit × 1 (P03961) K POTASSIUM ION × 3 9Y0 (2R)-3-(((2-aminoethoxy)(hydroxy)phosphoryl)oxy)-2-(palmitoyloxy)propyl (E)-octadec-9-enoate × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;20 mM Tris pH 7.4, 100 mM KCl, and 0.5 mM TCEP, 2 mM MgCl2, 1 mM ATP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.58 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.

24 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KDPF_ECOLI
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–29; UniProt 1–29

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 9zwn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9zwn
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9zwn
Deposition date deposition_date2026-01-03
Structure title titleHigh-resolution cryo-EM structure of KdpFABC in the E2P state in lipid nanodisc
Keywords keywordsP-type ATPase, potassium channel transporter pump, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.22
Radius of gyration Rg (electron density) rg_electron42.72
Forward intensity I(0) i0319671000.00
Molecular weight molecular_weight154720.0 kDa
Excluded volume excluded_volume197560 ų
Envelope volume envelope_volume250180 ų
Hydration-shell volume shell_volume52422 ų
Envelope diameter envelope_diameter163.2
Shell Rg shell_rg43.47
Envelope Rg envelope_rg43.60
Shape Rg shape_rg42.78
Total Rg total_rg42.55
Total atoms total_atoms10865
Residues n_residues1444
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 dmax152.2
Rg (real space) rg_real43.76
Rg uncertainty (real space) rg_real_error1.90
I(0) (real space) i0_real3.1970e+08
I(0) uncertainty (real space) i0_real_error6.2280e+06
Rg (reciprocal space) rg_reciprocal43.23
I(0) (reciprocal space) i0_reciprocal319500000.0000
Solution quality estimate total_estimate0.7840
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.0
Skewness Skewness skewness0.641
Kurtosis Kurtosis kurtosis-0.156
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha47460000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.661; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.727; Smooth: 0.476

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)