3c3q

ALIX Bro1-domain:CHMIP4B co-crystal structure

Method: X-RAY DIFFRACTION Dmax: 97.9 Å Quality: REASONABLE

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–359 Fragment:BRO1 domain (UNP residues 1-359) Charged multivesicular body protein 4b peptide × 1 (Q9H444) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;277 K;15% PEG 8,000, 100mM Na MES pH 6.5, 200mM Na Acetate, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.10 Å R-free 0.290

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

Charged multivesicular body protein 4b peptide

OrganismNot specified

UniProt Q9H444

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 207–224 Not recorded Programmed cell death 6-interacting protein × 1 (Q8WUM4) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;277 K;15% PEG 8,000, 100mM Na MES pH 6.5, 200mM Na Acetate, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.10 Å R-free 0.290

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 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CHM4B_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–18; UniProt 207–224

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 3c3q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3c3q
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3c3q
Deposition date deposition_date2008-01-28
Structure title titleALIX Bro1-domain:CHMIP4B co-crystal structure
Keywords keywords;ALIX CHMP4B BRO1 amphipathic-helix, Cataract, Disease mutation, Protein transport, Transport, Apoptosis, Host-virus interaction, TRANSPORT PROTEIN ;; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.11
Radius of gyration Rg (electron density) rg_electron25.65
Forward intensity I(0) i028950100.00
Molecular weight molecular_weight42032.0 kDa
Excluded volume excluded_volume52945 ų
Envelope volume envelope_volume66038 ų
Hydration-shell volume shell_volume23163 ų
Envelope diameter envelope_diameter102.6
Shell Rg shell_rg30.48
Envelope Rg envelope_rg26.37
Shape Rg shape_rg25.67
Total Rg total_rg26.17
Total atoms total_atoms2958
Residues n_residues375
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 dmax97.9
Rg (real space) rg_real26.42
Rg uncertainty (real space) rg_real_error0.96
I(0) (real space) i0_real2.8950e+07
I(0) uncertainty (real space) i0_real_error4.7560e+05
Rg (reciprocal space) rg_reciprocal26.32
I(0) (reciprocal space) i0_reciprocal28950000.0000
Solution quality estimate total_estimate0.5977
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.1
Skewness Skewness skewness0.678
Kurtosis Kurtosis kurtosis0.108
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7356000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.524; Stabil: 1.000; Sysdev: 0.221; Positv: 1.000; Valcen: 0.550; Smooth: 0.982

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id3c3qA00
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)