2j9u

2 Angstrom X-ray structure of the yeast ESCRT-I Vps28 C-terminus in complex with the NZF-N domain from ESCRT-II

Method: X-RAY DIFFRACTION Dmax: 73.4 Å Quality: EXCELLENT

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 148–242 Fragment:RESIDUES 148-242 VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 36 × 1 (Q06696) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.4;20% ETHANOL, 0.1M KCL, pH 7.40 Resolution 2.00 Å R-free 0.260
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 148–242 Fragment:RESIDUES 148-242 VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 36 × 1 (Q06696) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.4;20% ETHANOL, 0.1M KCL, pH 7.40 Resolution 2.00 Å R-free 0.260

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 25 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 2–96; UniProt 148–242 Author chain C; PDBConstruct 2–96; UniProt 148–242

VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 36

SACCHAROMYCES CEREVISIAE

UniProt Q06696

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 110–171 Fragment:RESIDUES 110-176 VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 28 × 1 (Q02767) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.4;20% ETHANOL, 0.1M KCL, pH 7.40 Resolution 2.00 Å R-free 0.260
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 110–171 Fragment:RESIDUES 110-176 VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 28 × 1 (Q02767) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.4;20% ETHANOL, 0.1M KCL, pH 7.40 Resolution 2.00 Å R-free 0.260

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VPS36_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 10–71; UniProt 110–171 Author chain D; PDBConstruct 10–71; UniProt 110–171

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 2j9u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2j9u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2j9u
Deposition date deposition_date2006-11-16
Structure title title2 Angstrom X-ray structure of the yeast ESCRT-I Vps28 C-terminus in complex with the NZF-N domain from ESCRT-II
Keywords keywordsZINC-FINGER, METAL-BINDING, 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_guinier22.76
Radius of gyration Rg (electron density) rg_electron21.71
Forward intensity I(0) i017124900.00
Molecular weight molecular_weight32060.0 kDa
Excluded volume excluded_volume40481 ų
Envelope volume envelope_volume50316 ų
Hydration-shell volume shell_volume20086 ų
Envelope diameter envelope_diameter74.3
Shell Rg shell_rg27.59
Envelope Rg envelope_rg21.75
Shape Rg shape_rg21.70
Total Rg total_rg22.58
Total atoms total_atoms2244
Residues n_residues282
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 dmax73.4
Rg (real space) rg_real22.74
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real1.7120e+07
I(0) uncertainty (real space) i0_real_error2.6130e+05
Rg (reciprocal space) rg_reciprocal22.75
I(0) (reciprocal space) i0_reciprocal17120000.0000
Solution quality estimate total_estimate0.9068
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.6
Skewness Skewness skewness0.284
Kurtosis Kurtosis kurtosis-0.460
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3023000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.935; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd2j9ua_
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
Domain ID domain_idd2j9ub1
Class classg — Small proteins
Fold Fold foldg.41 — Rubredoxin-like
Superfamily Superfamily superfamilyg.41.11 — Ran binding protein zinc finger-like
Family Family familyg.41.11.1 — Ran binding protein zinc finger-like
Domain ID domain_idd2j9uc_
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
Domain ID domain_idd2j9ud_
Class classg — Small proteins
Fold Fold foldg.41 — Rubredoxin-like
Superfamily Superfamily superfamilyg.41.11 — Ran binding protein zinc finger-like
Family Family familyg.41.11.1 — Ran binding protein zinc finger-like

CATH v4.4 (4 domains)

Domain ID domain_id2j9uA00
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
Domain ID domain_id2j9uB00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily380 — Zn-finger domain of Sec23/24
Domain ID domain_id2j9uC00
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
Domain ID domain_id2j9uD00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily380 — Zn-finger domain of Sec23/24

8. Citations (1)

9. Files and Curves (10)