7nnp

Rb-loaded cryo-EM structure of the E1-ATP KdpFABC complex.

Method: ELECTRON MICROSCOPY Dmax: 144.2 Å Quality: GOOD

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

Potassium-transporting ATPase potassium-binding subunit

Escherichia coli

UniProt A0A2S5ZPF1

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:G232D Potassium-transporting ATPase KdpC subunit × 1 (A0A037YI39) Potassium-transporting ATPase KdpF subunit × 1 (P36937) Potassium-transporting ATPase ATP-binding subunit × 1 (A0A024L5I2) RB RUBIDIUM ION × 8 CDL CARDIOLIPIN × 2 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;10 mM Tris-HCl pH 8, 10 mM MgCl2, 10 mM NaCl and 0.0125% DDM cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.20 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.

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

View Construct and Data Evidence
UniProt name A0A2S5ZPF1_ECOLX
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–557; UniProt 1–557

Potassium-transporting ATPase KdpC subunit

Escherichia coli

UniProt A0A037YI39

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 (A0A2S5ZPF1) Potassium-transporting ATPase KdpF subunit × 1 (P36937) Potassium-transporting ATPase ATP-binding subunit × 1 (A0A024L5I2) RB RUBIDIUM ION × 8 CDL CARDIOLIPIN × 2 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;10 mM Tris-HCl pH 8, 10 mM MgCl2, 10 mM NaCl and 0.0125% DDM cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.20 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.

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

View Construct and Data Evidence
UniProt name A0A037YI39_ECOLX
Isoform
PDB entities 2
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 1–27 Not recorded Potassium-transporting ATPase potassium-binding subunit × 1 (A0A2S5ZPF1) Potassium-transporting ATPase KdpC subunit × 1 (A0A037YI39) Potassium-transporting ATPase ATP-binding subunit × 1 (A0A024L5I2) RB RUBIDIUM ION × 8 CDL CARDIOLIPIN × 2 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;10 mM Tris-HCl pH 8, 10 mM MgCl2, 10 mM NaCl and 0.0125% DDM cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.20 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 3
Chains and sequence ranges Author chain D; PDBConstruct 1–27; UniProt 1–27

Potassium-transporting ATPase ATP-binding subunit

Escherichia coli

UniProt A0A024L5I2

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 (A0A2S5ZPF1) Potassium-transporting ATPase KdpC subunit × 1 (A0A037YI39) Potassium-transporting ATPase KdpF subunit × 1 (P36937) RB RUBIDIUM ION × 8 CDL CARDIOLIPIN × 2 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;10 mM Tris-HCl pH 8, 10 mM MgCl2, 10 mM NaCl and 0.0125% DDM cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.20 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.

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

View Construct and Data Evidence
UniProt name A0A024L5I2_ECOLX
Isoform
PDB entities 4
Chains and sequence ranges Author chain B; PDBConstruct 1–682; UniProt 1–682

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 7nnp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7nnp
Deposition date deposition_date2021-02-25
Structure title titleRb-loaded cryo-EM structure of the E1-ATP KdpFABC complex.
Keywords keywordsP-type ATPase, superfamily of K+ transporters (SKT), Rb substitution, intersubunit tunnel, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.48
Radius of gyration Rg (electron density) rg_electron40.69
Forward intensity I(0) i0331509000.00
Molecular weight molecular_weight158600.0 kDa
Excluded volume excluded_volume202700 ų
Envelope volume envelope_volume247410 ų
Hydration-shell volume shell_volume53068 ų
Envelope diameter envelope_diameter156.0
Shell Rg shell_rg43.37
Envelope Rg envelope_rg41.46
Shape Rg shape_rg40.79
Total Rg total_rg40.45
Total atoms total_atoms11096
Residues n_residues1456
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 dmax144.2
Rg (real space) rg_real41.83
Rg uncertainty (real space) rg_real_error1.83
I(0) (real space) i0_real3.3150e+08
I(0) uncertainty (real space) i0_real_error6.4980e+06
Rg (reciprocal space) rg_reciprocal41.49
I(0) (reciprocal space) i0_reciprocal331400000.0000
Solution quality estimate total_estimate0.8222
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.9
Skewness Skewness skewness0.562
Kurtosis Kurtosis kurtosis-0.250
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha51680000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.743; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.868; Smooth: 0.587

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id7nnpB01
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 (2)

9. Files and Curves (10)