4dl0

Crystal Structure of the heterotrimeric EGChead Peripheral Stalk Complex of the Yeast Vacuolar ATPase

Method: X-RAY DIFFRACTION Dmax: 234.4 Å Quality: REASONABLE

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

V-type proton ATPase subunit C

Saccharomyces cerevisiae

UniProt P31412

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain I; UniProt 158–277 Fragment:C subunit head domain, UNP residues 158-277 V-type proton ATPase subunit G × 1 (P48836) V-type proton ATPase subunit E × 1 (P22203) SO4 SULFATE ION × 4 PBM TRIMETHYL LEAD ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;292 K;0.1 M Lithium Sulfate, 0.1 M MES, 20% PEG mme 2000, 0.15 M Glycine, pH 6, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 2.90 Å R-free 0.257
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 158–277 Fragment:C subunit head domain, UNP residues 158-277 V-type proton ATPase subunit G × 1 (P48836) V-type proton ATPase subunit E × 1 (P22203) SO4 SULFATE ION × 4 PBM TRIMETHYL LEAD ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;292 K;0.1 M Lithium Sulfate, 0.1 M MES, 20% PEG mme 2000, 0.15 M Glycine, pH 6, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 2.90 Å R-free 0.257

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.

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATC_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 11–130; UniProt 158–277 Author chain I; PDBConstruct 11–130; UniProt 158–277

V-type proton ATPase subunit G

Saccharomyces cerevisiae

UniProt P48836

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain K; UniProt 1–114 Not recorded V-type proton ATPase subunit C × 1 (P31412) V-type proton ATPase subunit E × 1 (P22203) SO4 SULFATE ION × 4 PBM TRIMETHYL LEAD ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;292 K;0.1 M Lithium Sulfate, 0.1 M MES, 20% PEG mme 2000, 0.15 M Glycine, pH 6, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 2.90 Å R-free 0.257
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain G; UniProt 1–114 Not recorded V-type proton ATPase subunit C × 1 (P31412) V-type proton ATPase subunit E × 1 (P22203) SO4 SULFATE ION × 4 PBM TRIMETHYL LEAD ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;292 K;0.1 M Lithium Sulfate, 0.1 M MES, 20% PEG mme 2000, 0.15 M Glycine, pH 6, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 2.90 Å R-free 0.257

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.

20 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATG_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain G; PDBConstruct 6–119; UniProt 1–114 Author chain K; PDBConstruct 6–119; UniProt 1–114

V-type proton ATPase subunit E

Saccharomyces cerevisiae

UniProt P22203

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain J; UniProt 1–233 Not recorded V-type proton ATPase subunit C × 1 (P31412) V-type proton ATPase subunit G × 1 (P48836) SO4 SULFATE ION × 4 PBM TRIMETHYL LEAD ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;292 K;0.1 M Lithium Sulfate, 0.1 M MES, 20% PEG mme 2000, 0.15 M Glycine, pH 6, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 2.90 Å R-free 0.257
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 1–233 Not recorded V-type proton ATPase subunit C × 1 (P31412) V-type proton ATPase subunit G × 1 (P48836) SO4 SULFATE ION × 4 PBM TRIMETHYL LEAD ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;292 K;0.1 M Lithium Sulfate, 0.1 M MES, 20% PEG mme 2000, 0.15 M Glycine, pH 6, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 2.90 Å R-free 0.257

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 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATE_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–233; UniProt 1–233 Author chain J; PDBConstruct 1–233; UniProt 1–233

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 4dl0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4dl0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4dl0
Deposition date deposition_date2012-02-05
Structure title titleCrystal Structure of the heterotrimeric EGChead Peripheral Stalk Complex of the Yeast Vacuolar ATPase
Keywords keywordscoiled-coil, heterotrimer, peripheral stalk, stator complex, hydrolase, ion transport, Vacuolar ATPase, vacuolar membrane; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier62.92
Radius of gyration Rg (electron density) rg_electron65.34
Forward intensity I(0) i0150616000.00
Molecular weight molecular_weight101640.0 kDa
Excluded volume excluded_volume127390 ų
Envelope volume envelope_volume214250 ų
Hydration-shell volume shell_volume32492 ų
Envelope diameter envelope_diameter210.7
Shell Rg shell_rg49.26
Envelope Rg envelope_rg63.09
Shape Rg shape_rg65.33
Total Rg total_rg64.87
Total atoms total_atoms7104
Residues n_residues890
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 dmax234.4
Rg (real space) rg_real64.52
Rg uncertainty (real space) rg_real_error3.90
I(0) (real space) i0_real1.5060e+08
I(0) uncertainty (real space) i0_real_error3.2240e+06
Rg (reciprocal space) rg_reciprocal61.45
I(0) (reciprocal space) i0_reciprocal149800000.0000
Solution quality estimate total_estimate0.6027
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks4
Primary peak position r_peak_primary28.1
Skewness Skewness skewness0.462
Kurtosis Kurtosis kurtosis-0.966
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0009
Highest regularization parameter α highest_alpha5888000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.019; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.026; Smooth: 0.754

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd4dl0e1
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.36 — V-type ATPase peripheral stalk subunit E coiled coil
Family Family familyh.1.36.1 — V-type ATPase peripheral stalk subunit E coiled coil
Domain ID domain_idd4dl0e2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.81 — FwdE/GAPDH domain-like
Superfamily Superfamily superfamilyd.81.4 — V-type ATPase subunit E-like
Family Family familyd.81.4.1 — V-type ATPase subunit E C-terminal domain
Domain ID domain_idd4dl0g_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.37 — V-type ATPase peripheral stalk subunit G coiled coil
Family Family familyh.1.37.1 — V-type ATPase peripheral stalk subunit G coiled coil
Domain ID domain_idd4dl0j1
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.36 — V-type ATPase peripheral stalk subunit E coiled coil
Family Family familyh.1.36.1 — V-type ATPase peripheral stalk subunit E coiled coil
Domain ID domain_idd4dl0j2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.81 — FwdE/GAPDH domain-like
Superfamily Superfamily superfamilyd.81.4 — V-type ATPase subunit E-like
Family Family familyd.81.4.1 — V-type ATPase subunit E C-terminal domain
Domain ID domain_idd4dl0k_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.37 — V-type ATPase peripheral stalk subunit G coiled coil
Family Family familyh.1.37.1 — V-type ATPase peripheral stalk subunit G coiled coil

CATH v4.4 (6 domains)

Domain ID domain_id4dl0C00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily100
Domain ID domain_id4dl0E02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology2320 — hypothetical protein PF0899 fold
Homologous superfamily homologous superfamily30 — ATP synthase, E subunit, C-terminal
Domain ID domain_id4dl0G00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily2950
Domain ID domain_id4dl0I00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily100
Domain ID domain_id4dl0J02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology2320 — hypothetical protein PF0899 fold
Homologous superfamily homologous superfamily30 — ATP synthase, E subunit, C-terminal
Domain ID domain_id4dl0K00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily2950

8. Citations (1)

9. Files and Curves (10)