1obx

Crystal structure of the complex of PDZ2 of syntenin with an interleukin 5 receptor alpha peptide.

Method: X-RAY DIFFRACTION Dmax: 43.6 Å Quality: GOOD

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

SYNTENIN 1

HOMO SAPIENS

UniProt O00560

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 197–270 Fragment:PDZ2, RESIDUES 197-270 INTERLEUKIN 5 RECEPTOR ALPHA × 2 (Q01344) CO COBALT (II) ION × 4 SO4 SULFATE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;SITTING DROP 0.1 M HEPES, PH 7.0, 1.6 M AMMONIUM SULFATE, 20 MM COCL2, 0.2 M MGSO4 WITH MICROSEEDIN Resolution 1.35 Å R-free 0.212

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.

64 other PDB entries and 186 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SDB1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–79; UniProt 197–270

INTERLEUKIN 5 RECEPTOR ALPHA

OrganismNot specified

UniProt Q01344

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 413–420 Fragment:LAST 8 RESIDUES, RESIDUES 413-420 SYNTENIN 1 × 2 (O00560) CO COBALT (II) ION × 4 SO4 SULFATE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;SITTING DROP 0.1 M HEPES, PH 7.0, 1.6 M AMMONIUM SULFATE, 20 MM COCL2, 0.2 M MGSO4 WITH MICROSEEDIN Resolution 1.35 Å R-free 0.212

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.

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IL5R_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–8; UniProt 413–420

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 1obx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1obx
Deposition date deposition_date2003-01-31
Structure title titleCrystal structure of the complex of PDZ2 of syntenin with an interleukin 5 receptor alpha peptide.
Keywords keywordsCELL ADHESION, ADHESION-COMPLEX, PDZ DOMAIN, SIGNAL TRANSDUCTION, NUCLEAR PROTEIN; CELL ADHESION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier13.14
Radius of gyration Rg (electron density) rg_electron11.42
Forward intensity I(0) i01864200.00
Molecular weight molecular_weight8690.0 kDa
Excluded volume excluded_volume10649 ų
Envelope volume envelope_volume11819 ų
Hydration-shell volume shell_volume8996 ų
Envelope diameter envelope_diameter42.1
Shell Rg shell_rg16.87
Envelope Rg envelope_rg11.71
Shape Rg shape_rg11.33
Total Rg total_rg12.98
Total atoms total_atoms598
Residues n_residues78
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 dmax43.6
Rg (real space) rg_real13.03
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real1.8640e+06
I(0) uncertainty (real space) i0_real_error1.9060e+04
Rg (reciprocal space) rg_reciprocal13.04
I(0) (reciprocal space) i0_reciprocal1864000.0000
Solution quality estimate total_estimate0.8585
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.2
Skewness Skewness skewness0.063
Kurtosis Kurtosis kurtosis-0.260
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha359100.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.724; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.987

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1obxa_
Class classb — All beta proteins
Fold Fold foldb.36 — PDZ domain-like
Superfamily Superfamily superfamilyb.36.1 — PDZ domain-like
Family Family familyb.36.1.1 — PDZ domain

CATH v4.4 (1 domains)

Domain ID domain_id1obxA00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology42 — Pdz3 Domain
Homologous superfamily homologous superfamily10 — PDZ domain

8. Citations (1)

9. Files and Curves (10)