2j9v

2 Angstrom X-ray structure of the yeast ESCRT-I Vps28 C-terminus

Method: X-RAY DIFFRACTION Dmax: 55.5 Å Quality: REASONABLE

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

VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 28

SACCHAROMYCES CEREVISIAE

UniProt Q02767

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 148–242 Fragment:RESIDUES 148-242 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.6;4% PEG 400, 0.1M LITHIUM SULPHATE, 0.1M SODIUM CITRATE (PH5.6), pH 5.60 Resolution 2.00 Å R-free 0.255

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.

6 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VPS28_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–99; UniProt 148–242

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 2j9v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2j9v
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2j9v
Deposition date deposition_date2006-11-16
Structure title title2 Angstrom X-ray structure of the yeast ESCRT-I Vps28 C-terminus
Keywords keywordsNZF FINGER, HIV BUDDING, PROTEIN TRANSPORT, VPS, MVB, CHMP, ESCRT, VPS36, VPS28, TRANSPORT; PROTEIN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.46
Radius of gyration Rg (electron density) rg_electron14.03
Forward intensity I(0) i02576400.00
Molecular weight molecular_weight11548.0 kDa
Excluded volume excluded_volume14648 ų
Envelope volume envelope_volume16587 ų
Hydration-shell volume shell_volume10594 ų
Envelope diameter envelope_diameter53.8
Shell Rg shell_rg19.17
Envelope Rg envelope_rg14.51
Shape Rg shape_rg14.02
Total Rg total_rg15.21
Total atoms total_atoms816
Residues n_residues99
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 dmax55.5
Rg (real space) rg_real15.50
Rg uncertainty (real space) rg_real_error0.41
I(0) (real space) i0_real2.5760e+06
I(0) uncertainty (real space) i0_real_error3.0500e+04
Rg (reciprocal space) rg_reciprocal15.49
I(0) (reciprocal space) i0_reciprocal2576000.0000
Solution quality estimate total_estimate0.5989
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.9
Skewness Skewness skewness0.473
Kurtosis Kurtosis kurtosis0.053
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha472400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.588; Stabil: 1.000; Sysdev: 0.368; Positv: 1.000; Valcen: 0.912; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2j9va_
Class classa — All alpha proteins
Fold Fold folda.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamilya.24.28 — VPS28 C-terminal domain-like
Family Family familya.24.28.1 — VPS28 C-terminal domain-like

CATH v4.4 (1 domains)

Domain ID domain_id2j9vA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily1130 — Vps28 C-terminal domain

8. Citations (1)

9. Files and Curves (10)