7uzk

Rat Kidney V1 complex lacking subunit H with SidK and NCOA7B, State 1

Method: ELECTRON MICROSCOPY Dmax: 201.4 Å Quality: REASONABLE

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

ATPase H+-transporting V1 subunit A

OrganismNot specified

UniProt D4A133

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 × 19 PDB declaration: nonadecameric(19) Consistent with protein copy count Chain A; UniProt 1–617 Chain B; UniProt 1–617 Chain C; UniProt 1–617 Not recorded V-type proton ATPase subunit B, brain isoform × 3 (P62815) V-type proton ATPase subunit C 1 × 1 (Q5FVI6) ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit E 1 × 3 (Q6PCU2) V-type proton ATPase subunit F × 1 (P50408) V-type proton ATPase subunit G × 3 (B2GUV5) Effector SidK × 3 (Q5ZWW6) Nuclear receptor coactivator 7B × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name D4A133_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–617; UniProt 1–617 Author chain B; PDBConstruct 1–617; UniProt 1–617 Author chain C; PDBConstruct 1–617; UniProt 1–617

V-type proton ATPase subunit B, brain isoform

OrganismNot specified

UniProt P62815

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 × 19 PDB declaration: nonadecameric(19) Consistent with protein copy count Chain D; UniProt 1–511 Chain E; UniProt 1–511 Chain F; UniProt 1–511 Not recorded ATPase H+-transporting V1 subunit A × 3 (D4A133) V-type proton ATPase subunit C 1 × 1 (Q5FVI6) ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit E 1 × 3 (Q6PCU2) V-type proton ATPase subunit F × 1 (P50408) V-type proton ATPase subunit G × 3 (B2GUV5) Effector SidK × 3 (Q5ZWW6) Nuclear receptor coactivator 7B × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATB2_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–511; UniProt 1–511 Author chain E; PDBConstruct 1–511; UniProt 1–511 Author chain F; PDBConstruct 1–511; UniProt 1–511

V-type proton ATPase subunit C 1

OrganismNot specified

UniProt Q5FVI6

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 × 19 PDB declaration: nonadecameric(19) Consistent with protein copy count Chain G; UniProt 1–382 Not recorded ATPase H+-transporting V1 subunit A × 3 (D4A133) V-type proton ATPase subunit B, brain isoform × 3 (P62815) ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit E 1 × 3 (Q6PCU2) V-type proton ATPase subunit F × 1 (P50408) V-type proton ATPase subunit G × 3 (B2GUV5) Effector SidK × 3 (Q5ZWW6) Nuclear receptor coactivator 7B × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATC1_RAT
Isoform
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 1–382; UniProt 1–382

ATPase H+-transporting V1 subunit D

OrganismNot specified

UniProt Q6P503

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 × 19 PDB declaration: nonadecameric(19) Consistent with protein copy count Chain H; UniProt 1–247 Not recorded ATPase H+-transporting V1 subunit A × 3 (D4A133) V-type proton ATPase subunit B, brain isoform × 3 (P62815) V-type proton ATPase subunit C 1 × 1 (Q5FVI6) V-type proton ATPase subunit E 1 × 3 (Q6PCU2) V-type proton ATPase subunit F × 1 (P50408) V-type proton ATPase subunit G × 3 (B2GUV5) Effector SidK × 3 (Q5ZWW6) Nuclear receptor coactivator 7B × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

19 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q6P503_RAT
Isoform
PDB entities 4
Chains and sequence ranges Author chain H; PDBConstruct 1–247; UniProt 1–247

V-type proton ATPase subunit E 1

OrganismNot specified

UniProt Q6PCU2

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 × 19 PDB declaration: nonadecameric(19) Consistent with protein copy count Chain I; UniProt 1–226 Chain J; UniProt 1–226 Chain K; UniProt 1–226 Not recorded ATPase H+-transporting V1 subunit A × 3 (D4A133) V-type proton ATPase subunit B, brain isoform × 3 (P62815) V-type proton ATPase subunit C 1 × 1 (Q5FVI6) ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit F × 1 (P50408) V-type proton ATPase subunit G × 3 (B2GUV5) Effector SidK × 3 (Q5ZWW6) Nuclear receptor coactivator 7B × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

19 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATE1_RAT
Isoform
PDB entities 5
Chains and sequence ranges Author chain I; PDBConstruct 1–226; UniProt 1–226 Author chain J; PDBConstruct 1–226; UniProt 1–226 Author chain K; PDBConstruct 1–226; UniProt 1–226

V-type proton ATPase subunit F

OrganismNot specified

UniProt P50408

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 × 19 PDB declaration: nonadecameric(19) Consistent with protein copy count Chain L; UniProt 1–119 Not recorded ATPase H+-transporting V1 subunit A × 3 (D4A133) V-type proton ATPase subunit B, brain isoform × 3 (P62815) V-type proton ATPase subunit C 1 × 1 (Q5FVI6) ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit E 1 × 3 (Q6PCU2) V-type proton ATPase subunit G × 3 (B2GUV5) Effector SidK × 3 (Q5ZWW6) Nuclear receptor coactivator 7B × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATF_RAT
Isoform
PDB entities 6
Chains and sequence ranges Author chain L; PDBConstruct 1–119; UniProt 1–119

V-type proton ATPase subunit G

OrganismNot specified

UniProt B2GUV5

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 × 19 PDB declaration: nonadecameric(19) Consistent with protein copy count Chain M; UniProt 1–118 Chain N; UniProt 1–118 Chain O; UniProt 1–118 Not recorded ATPase H+-transporting V1 subunit A × 3 (D4A133) V-type proton ATPase subunit B, brain isoform × 3 (P62815) V-type proton ATPase subunit C 1 × 1 (Q5FVI6) ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit E 1 × 3 (Q6PCU2) V-type proton ATPase subunit F × 1 (P50408) Effector SidK × 3 (Q5ZWW6) Nuclear receptor coactivator 7B × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B2GUV5_RAT
Isoform
PDB entities 7
Chains and sequence ranges Author chain M; PDBConstruct 1–118; UniProt 1–118 Author chain N; PDBConstruct 1–118; UniProt 1–118 Author chain O; PDBConstruct 1–118; UniProt 1–118

Effector SidK

Legionella pneumophila

UniProt Q5ZWW6

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 × 19 PDB declaration: nonadecameric(19) Consistent with protein copy count Chain Q; UniProt 1–280 Chain R; UniProt 1–280 Chain S; UniProt 1–280 Not recorded ATPase H+-transporting V1 subunit A × 3 (D4A133) V-type proton ATPase subunit B, brain isoform × 3 (P62815) V-type proton ATPase subunit C 1 × 1 (Q5FVI6) ATPase H+-transporting V1 subunit D × 1 (Q6P503) V-type proton ATPase subunit E 1 × 3 (Q6PCU2) V-type proton ATPase subunit F × 1 (P50408) V-type proton ATPase subunit G × 3 (B2GUV5) Nuclear receptor coactivator 7B × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 Q5ZWW6_LEGPH
Isoform
PDB entities 8
Chains and sequence ranges Author chain Q; PDBConstruct 1–280; UniProt 1–280 Author chain R; PDBConstruct 1–280; UniProt 1–280 Author chain S; PDBConstruct 1–280; UniProt 1–280

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 7uzk

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7uzk
Deposition date deposition_date2022-05-09
最后修订 last_revision2023-11-22
Structure title titleRat Kidney V1 complex lacking subunit H with SidK and NCOA7B, State 1
Keywords keywordsV-ATPase, Complex, Membrane protein, PROTON TRANSPORT; PROTON TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier60.11
Radius of gyration Rg (electron density) rg_electron59.77
Forward intensity I(0) i05700690000.00
Molecular weight molecular_weight643880.0 kDa
Excluded volume excluded_volume809310 ų
Envelope volume envelope_volume1217900 ų
Hydration-shell volume shell_volume161500 ų
Envelope diameter envelope_diameter204.8
Shell Rg shell_rg66.77
Envelope Rg envelope_rg59.72
Shape Rg shape_rg59.76
Total Rg total_rg59.94
Total atoms total_atoms45246
Residues n_residues5702
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 dmax201.4
Rg (real space) rg_real59.87
Rg uncertainty (real space) rg_real_error1.89
I(0) (real space) i0_real5.7010e+09
I(0) uncertainty (real space) i0_real_error1.1930e+08
Rg (reciprocal space) rg_reciprocal60.29
I(0) (reciprocal space) i0_reciprocal5704000000.0000
Solution quality estimate total_estimate0.6404
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary69.7
Skewness Skewness skewness0.243
Kurtosis Kurtosis kurtosis-0.378
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha907500000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.821; Stabil: 1.000; Sysdev: 0.025; Positv: 1.000; Valcen: 0.948; Smooth: 0.836

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)