4efa

Crystal Structure of the Heterotrimeric EGChead Peripheral Stalk Complex of the Yeast Vacuolar ATPase - second conformation

Method: X-RAY DIFFRACTION Dmax: 185.9 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 C; UniProt 158–277 Fragment:UNP Residues 158-277 V-type proton ATPase subunit G × 1 (P48836) V-type proton ATPase subunit E × 1 (P22203) SO4 SULFATE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;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 2.82 Å R-free 0.277

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 18 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

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 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 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;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 2.82 Å R-free 0.277

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 23 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

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 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 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;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 2.82 Å R-free 0.277

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 24 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

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 4efa

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4efa
Deposition date deposition_date2012-03-29
Structure title titleCrystal Structure of the Heterotrimeric EGChead Peripheral Stalk Complex of the Yeast Vacuolar ATPase - second conformation
Keywords keywordsheterotrimer, peripheral stalk, vacuolar ATPase, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier60.87
Radius of gyration Rg (electron density) rg_electron63.58
Forward intensity I(0) i034672900.00
Molecular weight molecular_weight48513.0 kDa
Excluded volume excluded_volume61070 ų
Envelope volume envelope_volume116590 ų
Hydration-shell volume shell_volume19081 ų
Envelope diameter envelope_diameter192.0
Shell Rg shell_rg44.14
Envelope Rg envelope_rg61.33
Shape Rg shape_rg63.61
Total Rg total_rg62.65
Total atoms total_atoms3405
Residues n_residues426
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 dmax185.9
Rg (real space) rg_real62.40
Rg uncertainty (real space) rg_real_error2.71
I(0) (real space) i0_real3.4670e+07
I(0) uncertainty (real space) i0_real_error8.2620e+05
Rg (reciprocal space) rg_reciprocal59.44
I(0) (reciprocal space) i0_reciprocal34500000.0000
Solution quality estimate total_estimate0.5425
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary21.4
Skewness Skewness skewness0.395
Kurtosis Kurtosis kurtosis-1.125
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1226000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.015; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.004; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd4efae1
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_idd4efae2
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_idd4efag_
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 (3 domains)

Domain ID domain_id4efaC00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily100
Domain ID domain_id4efaE02
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_id4efaG00
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)