3r42

Crystal structure of the yeast vps23 UEV domain in complex with a vps27 PSDP peptide

Method: X-RAY DIFFRACTION Dmax: 61.4 Å Quality: GOOD

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

Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease

Saccharomyces cerevisiae

UniProt P25604

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–160 Fragment:N-terminal UEV domain (UNP residues 1-160) Mutation:C133A Vacuolar protein sorting-associated protein 27 × 1 (P40343) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.3;288 K;0.2 M sodium phosphate monobasic, 20% PEG3350, pH 7.3, VAPOR DIFFUSION, HANGING DROP, temperature 288K Resolution 1.87 Å R-free 0.203
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–160 Fragment:N-terminal UEV domain (UNP residues 1-160) Mutation:C133A Vacuolar protein sorting-associated protein 27 × 2 (P40343) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.3;288 K;0.2 M sodium phosphate monobasic, 20% PEG3350, pH 7.3, VAPOR DIFFUSION, HANGING DROP, temperature 288K Resolution 1.87 Å R-free 0.203

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 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name STP22_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–162; UniProt 1–160

Vacuolar protein sorting-associated protein 27

OrganismNot specified

UniProt P40343

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 445–453 Fragment:PSDP peptide (UNP residues 445-453) Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease × 1 (P25604) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.3;288 K;0.2 M sodium phosphate monobasic, 20% PEG3350, pH 7.3, VAPOR DIFFUSION, HANGING DROP, temperature 288K Resolution 1.87 Å R-free 0.203
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 445–453 Fragment:PSDP peptide (UNP residues 445-453) Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease × 2 (P25604) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.3;288 K;0.2 M sodium phosphate monobasic, 20% PEG3350, pH 7.3, VAPOR DIFFUSION, HANGING DROP, temperature 288K Resolution 1.87 Å R-free 0.203

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 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VPS27_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–9; UniProt 445–453

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 3r42

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3r42
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3r42
Deposition date deposition_date2011-03-17
Structure title titleCrystal structure of the yeast vps23 UEV domain in complex with a vps27 PSDP peptide
Keywords keywordsendosomal sorting, ESCRT, PROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.74
Radius of gyration Rg (electron density) rg_electron16.20
Forward intensity I(0) i06049140.00
Molecular weight molecular_weight18341.0 kDa
Excluded volume excluded_volume23159 ų
Envelope volume envelope_volume27090 ų
Hydration-shell volume shell_volume14364 ų
Envelope diameter envelope_diameter61.4
Shell Rg shell_rg21.99
Envelope Rg envelope_rg16.88
Shape Rg shape_rg16.20
Total Rg total_rg17.26
Total atoms total_atoms1295
Residues n_residues164
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 dmax61.4
Rg (real space) rg_real17.71
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real6.0490e+06
I(0) uncertainty (real space) i0_real_error6.7440e+04
Rg (reciprocal space) rg_reciprocal17.71
I(0) (reciprocal space) i0_reciprocal6049000.0000
Solution quality estimate total_estimate0.7675
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary55.7
Skewness Skewness skewness0.353
Kurtosis Kurtosis kurtosis0.052
Angular range angular_range— – 0.4500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1071000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.666; Stabil: 0.996; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3r42a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.20 — UBC-like
Superfamily Superfamily superfamilyd.20.1 — UBC-like
Family Family familyd.20.1.2 — UEV domain

CATH v4.4 (1 domains)

Domain ID domain_id3r42A00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology110 — Ubiquitin Conjugating Enzyme
Homologous superfamily homologous superfamily10 — Ubiquitin Conjugating Enzyme

8. Citations (1)

9. Files and Curves (10)