8xws

Structure of CXCR2 bound to CXCL5 (Ligand-receptor focused map)

Method: ELECTRON MICROSCOPY Dmax: 130.7 Å Quality: REASONABLE

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

C-X-C motif chemokine 5

Homo sapiens

UniProt P42830

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 37–114 Chain D; UniProt 37–114 Not recorded C-X-C chemokine receptor type 2 × 2 (P25025) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.06 Å

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CXCL5_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–78; UniProt 37–114 Author chain D; PDBConstruct 1–78; UniProt 37–114

C-X-C chemokine receptor type 2

Homo sapiens

UniProt P25025

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 C; UniProt 2–360 Chain R; UniProt 2–360 Not recorded C-X-C motif chemokine 5 × 2 (P42830) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.06 Å

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 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CXCR2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 58–416; UniProt 2–360 Author chain R; PDBConstruct 58–416; UniProt 2–360

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 8xws

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8xws
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8xws
Deposition date deposition_date2024-01-16
Structure title titleStructure of CXCR2 bound to CXCL5 (Ligand-receptor focused map)
Keywords keywordsGPCR, Arrestin, SIGNALING PROTEIN-IMMUNE SYSTEM complex; SIGNALING PROTEIN/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.48
Radius of gyration Rg (electron density) rg_electron38.50
Forward intensity I(0) i082189800.00
Molecular weight molecular_weight80444.0 kDa
Excluded volume excluded_volume104120 ų
Envelope volume envelope_volume142110 ų
Hydration-shell volume shell_volume33084 ų
Envelope diameter envelope_diameter140.9
Shell Rg shell_rg40.37
Envelope Rg envelope_rg38.33
Shape Rg shape_rg38.52
Total Rg total_rg38.58
Total atoms total_atoms5656
Residues n_residues730
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 dmax130.7
Rg (real space) rg_real38.02
Rg uncertainty (real space) rg_real_error1.17
I(0) (real space) i0_real8.2190e+07
I(0) uncertainty (real space) i0_real_error1.5160e+06
Rg (reciprocal space) rg_reciprocal37.69
I(0) (reciprocal space) i0_reciprocal82160000.0000
Solution quality estimate total_estimate0.5493
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary28.0
Skewness Skewness skewness0.541
Kurtosis Kurtosis kurtosis-0.421
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha11920000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.606; Stabil: 1.000; Sysdev: 0.000; Positv: 1.000; Valcen: 0.557; Smooth: 0.762

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)