6wlz

The V1 region of human V-ATPase in state 1 (focused refinement)

Method: ELECTRON MICROSCOPY Dmax: 183.3 Å Quality: REASONABLE

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

V-type proton ATPase catalytic subunit A

OrganismNot specified

UniProt P38606

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 × 17 PDB declaration: heptadecameric(17) 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 (P21281) SidK × 3 (Q5ZWW6) V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit F × 1 (Q16864) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATA_HUMAN
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 P21281

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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain D; UniProt 1–511 Chain E; UniProt 1–511 Chain F; UniProt 1–511 Not recorded V-type proton ATPase catalytic subunit A × 3 (P38606) SidK × 3 (Q5ZWW6) V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit F × 1 (Q16864) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATB2_HUMAN
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

SidK

OrganismNot specified

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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain X; UniProt 1–573 Chain Y; UniProt 1–573 Chain Z; UniProt 1–573 Not recorded V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit F × 1 (Q16864) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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 3
Chains and sequence ranges Author chain X; PDBConstruct 1–573; UniProt 1–573 Author chain Y; PDBConstruct 1–573; UniProt 1–573 Author chain Z; PDBConstruct 1–573; UniProt 1–573

V-type proton ATPase subunit E 1

OrganismNot specified

UniProt P36543

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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain H; UniProt 1–226 Chain I; UniProt 1–226 Chain J; UniProt 1–226 Not recorded V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) SidK × 3 (Q5ZWW6) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit F × 1 (Q16864) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATE1_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain H; PDBConstruct 1–226; UniProt 1–226 Author chain I; PDBConstruct 1–226; UniProt 1–226 Author chain J; PDBConstruct 1–226; UniProt 1–226

V-type proton ATPase subunit G 1

OrganismNot specified

UniProt O75348

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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain K; UniProt 1–118 Chain L; UniProt 1–118 Chain M; UniProt 1–118 Not recorded V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) SidK × 3 (Q5ZWW6) V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit D × 1 (Q9Y5K8) V-type proton ATPase subunit F × 1 (Q16864) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATG1_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain K; PDBConstruct 1–118; UniProt 1–118 Author chain L; PDBConstruct 1–118; UniProt 1–118 Author chain M; PDBConstruct 1–118; UniProt 1–118

V-type proton ATPase subunit D

OrganismNot specified

UniProt Q9Y5K8

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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain G; UniProt 1–247 Not recorded V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) SidK × 3 (Q5ZWW6) V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit F × 1 (Q16864) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATD_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain G; PDBConstruct 1–247; UniProt 1–247

V-type proton ATPase subunit F

OrganismNot specified

UniProt Q16864

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 × 17 PDB declaration: heptadecameric(17) Consistent with protein copy count Chain N; UniProt 1–119 Not recorded V-type proton ATPase catalytic subunit A × 3 (P38606) V-type proton ATPase subunit B, brain isoform × 3 (P21281) SidK × 3 (Q5ZWW6) V-type proton ATPase subunit E 1 × 3 (P36543) V-type proton ATPase subunit G 1 × 3 (O75348) V-type proton ATPase subunit D × 1 (Q9Y5K8) ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATF_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain N; PDBConstruct 1–119; UniProt 1–119

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 6wlz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6wlz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6wlz
Deposition date deposition_date2020-04-20
Structure title titleThe V1 region of human V-ATPase in state 1 (focused refinement)
Keywords keywordsV-ATPase, proton 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_guinier56.25
Radius of gyration Rg (electron density) rg_electron55.77
Forward intensity I(0) i04660750000.00
Molecular weight molecular_weight578970.0 kDa
Excluded volume excluded_volume726970 ų
Envelope volume envelope_volume1056900 ų
Hydration-shell volume shell_volume148980 ų
Envelope diameter envelope_diameter182.3
Shell Rg shell_rg64.26
Envelope Rg envelope_rg55.55
Shape Rg shape_rg55.75
Total Rg total_rg56.03
Total atoms total_atoms40656
Residues n_residues5139
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 dmax183.3
Rg (real space) rg_real55.98
Rg uncertainty (real space) rg_real_error1.17
I(0) (real space) i0_real4.6610e+09
I(0) uncertainty (real space) i0_real_error9.2000e+07
Rg (reciprocal space) rg_reciprocal56.46
I(0) (reciprocal space) i0_reciprocal4664000000.0000
Solution quality estimate total_estimate0.6506
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary72.0
Skewness Skewness skewness0.177
Kurtosis Kurtosis kurtosis-0.441
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha946200000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.852; Stabil: 1.000; Sysdev: 0.041; Positv: 1.000; Valcen: 0.959; Smooth: 0.815

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (11 domains)

Domain ID domain_idd6wlzd1
Class classb — All beta proteins
Fold Fold foldb.49 — Domain of alpha and beta subunits of F1 ATP synthase-like
Superfamily Superfamily superfamilyb.49.1 — N-terminal domain of alpha and beta (or A/B) subunits of rotary ATPases
Family Family familyb.49.1.0 — automated matches
Domain ID domain_idd6wlzd2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.0 — automated matches
Domain ID domain_idd6wlzd3
Class classa — All alpha proteins
Fold Fold folda.69 — Left-handed superhelix
Superfamily Superfamily superfamilya.69.1 — C-terminal domain of alpha and beta (or A/B) subunits of rotary ATPases
Family Family familya.69.1.0 — automated matches
Domain ID domain_idd6wlze1
Class classb — All beta proteins
Fold Fold foldb.49 — Domain of alpha and beta subunits of F1 ATP synthase-like
Superfamily Superfamily superfamilyb.49.1 — N-terminal domain of alpha and beta (or A/B) subunits of rotary ATPases
Family Family familyb.49.1.0 — automated matches
Domain ID domain_idd6wlze2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.0 — automated matches
Domain ID domain_idd6wlze3
Class classa — All alpha proteins
Fold Fold folda.69 — Left-handed superhelix
Superfamily Superfamily superfamilya.69.1 — C-terminal domain of alpha and beta (or A/B) subunits of rotary ATPases
Family Family familya.69.1.0 — automated matches
Domain ID domain_idd6wlzf1
Class classb — All beta proteins
Fold Fold foldb.49 — Domain of alpha and beta subunits of F1 ATP synthase-like
Superfamily Superfamily superfamilyb.49.1 — N-terminal domain of alpha and beta (or A/B) subunits of rotary ATPases
Family Family familyb.49.1.0 — automated matches
Domain ID domain_idd6wlzf2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.0 — automated matches
Domain ID domain_idd6wlzf3
Class classa — All alpha proteins
Fold Fold folda.69 — Left-handed superhelix
Superfamily Superfamily superfamilya.69.1 — C-terminal domain of alpha and beta (or A/B) subunits of rotary ATPases
Family Family familya.69.1.0 — automated matches
Domain ID domain_idd6wlzg_
Class classh — Coiled coil proteins
Fold Fold foldh.4 — Antiparallel coiled-coil
Superfamily Superfamily superfamilyh.4.20 — V-type ATPase central rotor subunit D
Family Family familyh.4.20.0 — automated matches
Domain ID domain_idd6wlzn_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.149 — AtpF-like
Superfamily Superfamily superfamilyc.149.1 — AtpF-like
Family Family familyc.149.1.0 — automated matches

CATH v4.4 (1 domains)

Domain ID domain_id6wlzG01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily3240

8. Citations (1)

9. Files and Curves (10)