7lc6

Cryo-EM Structure of KdpFABC in E2-P state with BeF3

Method: ELECTRON MICROSCOPY Dmax: 153.3 Å Quality: GOOD

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

Potassium-transporting ATPase potassium-binding subunit

Escherichia coli (strain K12)

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 Mutation:Q116R 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 × 1 9Y0 (2R)-3-(((2-aminoethoxy)(hydroxy)phosphoryl)oxy)-2-(palmitoyloxy)propyl (E)-octadec-9-enoate × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;The beryllium fluoride in the buffer was added to the protein mixture containing all other buffer components in the form of a pre-incubated mixture with the final concentrations 2.5 mM BeSO4 and 10 mM NaF. cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of protein mixture applied to grid. Blot time 4 seconds, blot force 0, no wait before plunging. Resolution 3.70 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 (strain K12)

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 Mutation:S162A 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 × 1 9Y0 (2R)-3-(((2-aminoethoxy)(hydroxy)phosphoryl)oxy)-2-(palmitoyloxy)propyl (E)-octadec-9-enoate × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;The beryllium fluoride in the buffer was added to the protein mixture containing all other buffer components in the form of a pre-incubated mixture with the final concentrations 2.5 mM BeSO4 and 10 mM NaF. cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of protein mixture applied to grid. Blot time 4 seconds, blot force 0, no wait before plunging. Resolution 3.70 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 (strain K12)

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 × 1 9Y0 (2R)-3-(((2-aminoethoxy)(hydroxy)phosphoryl)oxy)-2-(palmitoyloxy)propyl (E)-octadec-9-enoate × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;The beryllium fluoride in the buffer was added to the protein mixture containing all other buffer components in the form of a pre-incubated mixture with the final concentrations 2.5 mM BeSO4 and 10 mM NaF. cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of protein mixture applied to grid. Blot time 4 seconds, blot force 0, no wait before plunging. Resolution 3.70 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 (strain K12)

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 × 1 9Y0 (2R)-3-(((2-aminoethoxy)(hydroxy)phosphoryl)oxy)-2-(palmitoyloxy)propyl (E)-octadec-9-enoate × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;The beryllium fluoride in the buffer was added to the protein mixture containing all other buffer components in the form of a pre-incubated mixture with the final concentrations 2.5 mM BeSO4 and 10 mM NaF. cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of protein mixture applied to grid. Blot time 4 seconds, blot force 0, no wait before plunging. Resolution 3.70 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 7lc6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7lc6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7lc6
Deposition date deposition_date2021-01-09
Structure title titleCryo-EM Structure of KdpFABC in E2-P state with BeF3
Keywords keywordsP-type ATPase, ATP-dependent potassium pump, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.51
Radius of gyration Rg (electron density) rg_electron43.11
Forward intensity I(0) i0316764000.00
Molecular weight molecular_weight153420.0 kDa
Excluded volume excluded_volume195740 ų
Envelope volume envelope_volume254290 ų
Hydration-shell volume shell_volume52826 ų
Envelope diameter envelope_diameter165.1
Shell Rg shell_rg43.61
Envelope Rg envelope_rg43.97
Shape Rg shape_rg43.16
Total Rg total_rg42.94
Total atoms total_atoms21954
Residues n_residues1440
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 dmax153.3
Rg (real space) rg_real44.06
Rg uncertainty (real space) rg_real_error1.91
I(0) (real space) i0_real3.1680e+08
I(0) uncertainty (real space) i0_real_error6.7950e+06
Rg (reciprocal space) rg_reciprocal43.51
I(0) (reciprocal space) i0_reciprocal316600000.0000
Solution quality estimate total_estimate0.7798
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.3
Skewness Skewness skewness0.646
Kurtosis Kurtosis kurtosis-0.140
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha44130000.0000
Real-space data points n_real_points37
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: 0.673; Smooth: 0.475

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id7lc6B01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1110 — Calcium-transporting ATPase, cytoplasmic domain N
Homologous superfamily homologous superfamily10 — Calcium-transporting ATPase, cytoplasmic domain N

8. Citations (1)

9. Files and Curves (10)