2oew

Structure of ALIX/AIP1 Bro1 Domain

Method: X-RAY DIFFRACTION Dmax: 98.2 Å Quality: GOOD

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

Programmed cell death 6-interacting protein

Homo sapiens

UniProt Q8WUM4

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 1–359 Fragment:Bro1 Domain, residues 1-359 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;286 K;10% PEG 20000, 0.1M NaMES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 286K Resolution 2.55 Å R-free 0.274

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.

18 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PDC6I_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 22–380; UniProt 1–359

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 2oew

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2oew
Deposition date deposition_date2007-01-01
Structure title titleStructure of ALIX/AIP1 Bro1 Domain
Keywords keywordsTetratricopeptide repeat, TPR, 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_guinier26.14
Radius of gyration Rg (electron density) rg_electron25.71
Forward intensity I(0) i025843800.00
Molecular weight molecular_weight39921.0 kDa
Excluded volume excluded_volume50449 ų
Envelope volume envelope_volume63335 ų
Hydration-shell volume shell_volume22454 ų
Envelope diameter envelope_diameter104.5
Shell Rg shell_rg30.27
Envelope Rg envelope_rg26.42
Shape Rg shape_rg25.72
Total Rg total_rg26.22
Total atoms total_atoms2811
Residues n_residues358
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 dmax98.2
Rg (real space) rg_real26.50
Rg uncertainty (real space) rg_real_error1.03
I(0) (real space) i0_real2.5840e+07
I(0) uncertainty (real space) i0_real_error3.7160e+05
Rg (reciprocal space) rg_reciprocal26.39
I(0) (reciprocal space) i0_reciprocal25840000.0000
Solution quality estimate total_estimate0.7579
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.1
Skewness Skewness skewness0.701
Kurtosis Kurtosis kurtosis0.088
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6848000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.481; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.459; Smooth: 0.947

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2oewa_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.8 — TPR-like
Family Family familya.118.8.0 — automated matches

CATH v4.4 (1 domains)

Domain ID domain_id2oewA00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily280 — alix/aip1 like domains

8. Citations (1)

9. Files and Curves (10)