6oo2

Vps4 with Cyclic Peptide Bound in the Central Pore

Method: ELECTRON MICROSCOPY
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Vacuolar protein sorting-associated protein 4

Saccharomyces cerevisiae

UniProt P52917

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 19 Designed Cyclic Peptide × 1 Vacuolar protein sorting-associated protein VTA1 × 12 (Q06263) ADENOSINE-5'-DIPHOSPHATE × 5 BERYLLIUM TRIFLUORIDE ION × 3 MAGNESIUM ION × 4 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name VPS4_YEAST
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–337; UniProt 101–437 Author chain B; PDBConstruct 1–337; UniProt 101–437 Author chain C; PDBConstruct 1–337; UniProt 101–437 Author chain D; PDBConstruct 1–337; UniProt 101–437 Author chain E; PDBConstruct 1–337; UniProt 101–437 Author chain F; PDBConstruct 1–337; UniProt 101–437

Vacuolar protein sorting-associated protein VTA1

Saccharomyces cerevisiae

UniProt Q06263

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 19 Vacuolar protein sorting-associated protein 4 × 6 (P52917) Designed Cyclic Peptide × 1 ADENOSINE-5'-DIPHOSPHATE × 5 BERYLLIUM TRIFLUORIDE ION × 3 MAGNESIUM ION × 4 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name VTA1_YEAST
Isoform —
PDB entities 3
Chains and sequence ranges Author chain H; PDBConstruct 1–51; UniProt 280–330 Author chain I; PDBConstruct 1–51; UniProt 280–330 Author chain J; PDBConstruct 1–51; UniProt 280–330 Author chain K; PDBConstruct 1–51; UniProt 280–330 Author chain L; PDBConstruct 1–51; UniProt 280–330 Author chain M; PDBConstruct 1–51; UniProt 280–330 Author chain N; PDBConstruct 1–51; UniProt 280–330 Author chain O; PDBConstruct 1–51; UniProt 280–330 Author chain P; PDBConstruct 1–51; UniProt 280–330 Author chain Q; PDBConstruct 1–51; UniProt 280–330 Author chain R; PDBConstruct 1–51; UniProt 280–330 Author chain S; PDBConstruct 1–51; UniProt 280–330

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id6oo2
Deposition date deposition_date2019-04-22
Structure title titleVps4 with Cyclic Peptide Bound in the Central Pore
Keywords keywordsVps4, ESCRT, Vta1, AAA ATPase, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

6oo2__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

6oo2__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

6oo2__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)48.16 Å
Rg (electron density)47.30 Å
Total Rg47.28 Å
Atom count16691
Residues2443
Excluded volume290500 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 6oo2__assembly_1__model_1 nonadecameric (19) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (6)

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7. Citations (1)