1yx4

Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition

Method: SOLUTION NMR Dmax: 129.1 Å Quality: GOOD

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

26S proteasome non-ATPase regulatory subunit 4

Homo sapiens

UniProt P55036

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 192–306 Fragment:(poly)ubiquitin binding region No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.5;298 K;Ionic strength (raw mmCIF value) 100 mM NaCl;Pressure 1 NMR measurement conditions:pH 6.5;283 K;Ionic strength (raw mmCIF value) 100 mM NaCl;Pressure 1 NMR sample composition:0.35 mM S5a U-15N, 13C | 20 mM phosphate buffer pH 6.5, 100 mM NaCl, 10% D2O NMR sample composition:1 mM S5a U-15N | 20 mM phosphate buffer pH 6.5, 100 mM NaCl, 10% D2O NMR sample composition:0.5 mM S5a unlabeled | 20 mM phosphate buffer pH 6.5, 100 mM NaCl, 10% D2O NMR sample composition:0.5 mM S5a U-N15 and 50% Deuterated | 20 mM phosphate buffer pH 6.5, 100 mM NaCl, 10% D2O NMR sample composition:1 mM S5a U-C13 | 20 mM phosphate buffer pH 6.5, 100 mM NaCl, 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.

124 other PDB entries and 124 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSD4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 18–132; UniProt 192–306

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 1yx4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1yx4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1yx4
Deposition date deposition_date2005-02-19
Structure title titleStructure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition
Keywords keywordspolyubiquitin, proteasome, S5a, UIM, Hydrolase; HYDROLASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier36.34
Radius of gyration Rg (electron density) rg_electron36.46
Forward intensity I(0) i0567292000.00
Molecular weight molecular_weight179130.0 kDa
Excluded volume excluded_volume217000 ų
Envelope volume envelope_volume272830 ų
Hydration-shell volume shell_volume54605 ų
Envelope diameter envelope_diameter144.5
Shell Rg shell_rg46.32
Envelope Rg envelope_rg41.81
Shape Rg shape_rg36.44
Total Rg total_rg36.96
Total atoms total_atoms24255
Residues n_residues1680
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 dmax129.1
Rg (real space) rg_real36.54
Rg uncertainty (real space) rg_real_error1.74
I(0) (real space) i0_real5.6730e+08
I(0) uncertainty (real space) i0_real_error1.1280e+07
Rg (reciprocal space) rg_reciprocal36.42
I(0) (reciprocal space) i0_reciprocal567200000.0000
Solution quality estimate total_estimate0.7751
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary44.0
Skewness Skewness skewness0.317
Kurtosis Kurtosis kurtosis-0.274
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha822000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.727; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.893; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id1yx4A01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily3990

8. Citations (1)

9. Files and Curves (10)