3p9h

Crystal structure of the TSG101 UEV domain in complex with FA258 peptide

Method: X-RAY DIFFRACTION Dmax: 53.9 Å Quality: GOOD

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

Tumor susceptibility gene 101 protein

Homo sapiens

UniProt Q99816

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 2–145 Fragment:N-terminal UEV domain (UNP residues 2 to 145) Mutation:Mutation of 43VFNDGS48 to GG Gag polyprotein × 1 (Q9YP46) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;298 K;0.1M HEPES-NAOH (PH7.5), 25% PEG 3350, 0.2M SODIUM NITRATE , VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.80 Å R-free 0.253

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 43 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TS101_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–145; UniProt 2–145

Gag polyprotein

OrganismNot specified

UniProt Q9YP46

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 453–461 Fragment:Modified HIV-1 Gag PTAP Motif Non-standard monomer:Yes (specific site not provided by mmCIF) Tumor susceptibility gene 101 protein × 1 (Q99816) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;298 K;0.1M HEPES-NAOH (PH7.5), 25% PEG 3350, 0.2M SODIUM NITRATE , VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.80 Å R-free 0.253

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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q9YP46_9HIV1
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–10; UniProt 453–461

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 3p9h

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3p9h
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3p9h
Deposition date deposition_date2010-10-17
Structure title titleCrystal structure of the TSG101 UEV domain in complex with FA258 peptide
Keywords keywordsPROTEIN TRANSPORT, Ubiquitin; PROTEIN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.85
Radius of gyration Rg (electron density) rg_electron15.37
Forward intensity I(0) i05196930.00
Molecular weight molecular_weight17254.0 kDa
Excluded volume excluded_volume22004 ų
Envelope volume envelope_volume24958 ų
Hydration-shell volume shell_volume13792 ų
Envelope diameter envelope_diameter53.1
Shell Rg shell_rg21.08
Envelope Rg envelope_rg15.77
Shape Rg shape_rg15.36
Total Rg total_rg16.54
Total atoms total_atoms1216
Residues n_residues149
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 dmax53.9
Rg (real space) rg_real16.78
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real5.1970e+06
I(0) uncertainty (real space) i0_real_error5.4470e+04
Rg (reciprocal space) rg_reciprocal16.79
I(0) (reciprocal space) i0_reciprocal5197000.0000
Solution quality estimate total_estimate0.8159
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.6
Skewness Skewness skewness0.225
Kurtosis Kurtosis kurtosis-0.350
Angular range angular_range— – 0.4700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1183000.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.868; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3p9ha1
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
Domain ID domain_idd3p9ha2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id3p9hA00
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)