1kpq

Structure of the Tsg101 UEV domain

Method: SOLUTION NMR Dmax: 53.7 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–145 Fragment:UEV domain, residues 1-145 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 5.5;293 K;Ionic strength (raw mmCIF value) 50 mM NaCl;Pressure ambient NMR sample composition:~1.5 mM Tsg101 UEV; 20 mM sodium phosphate pH 5.5; 50 mM NaCl | 90% H2O/10% D2O Resolution not provided

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 1–145; UniProt 1–145

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 1kpq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1kpq
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1kpq
Deposition date deposition_date2002-01-02
Structure title titleStructure of the Tsg101 UEV domain
Keywords keywordsE2 FOLD, CELL CYCLE; CELL CYCLE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier16.57
Radius of gyration Rg (electron density) rg_electron15.94
Forward intensity I(0) i0740822000.00
Molecular weight molecular_weight247040.0 kDa
Excluded volume excluded_volume315750 ų
Envelope volume envelope_volume40014 ų
Hydration-shell volume shell_volume18576 ų
Envelope diameter envelope_diameter59.5
Shell Rg shell_rg24.29
Envelope Rg envelope_rg18.28
Shape Rg shape_rg15.94
Total Rg total_rg16.12
Total atoms total_atoms17415
Residues n_residues2160
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 dmax53.7
Rg (real space) rg_real16.51
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real7.4080e+08
I(0) uncertainty (real space) i0_real_error9.1500e+06
Rg (reciprocal space) rg_reciprocal16.51
I(0) (reciprocal space) i0_reciprocal740800000.0000
Solution quality estimate total_estimate0.8033
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.1
Skewness Skewness skewness0.203
Kurtosis Kurtosis kurtosis-0.350
Angular range angular_range— – 0.4800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha429300.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.814; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1kpqa_
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_id1kpqA00
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)