8xx7

Structure of CXCR2 bound to CXCL5 (CXCR2-CXCL5-Go Full map)

Method: ELECTRON MICROSCOPY Dmax: 195.2 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 × 10 PDB declaration: decameric(10) 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) Guanine nucleotide-binding protein G(o) subunit alpha × 2 (P09471) Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 2 (P62873) Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 2 (P59768) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.32 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 × 10 PDB declaration: decameric(10) 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) Guanine nucleotide-binding protein G(o) subunit alpha × 2 (P09471) Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 2 (P62873) Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 2 (P59768) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.32 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

Guanine nucleotide-binding protein G(o) subunit alpha

Homo sapiens

UniProt P09471

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 4–57 Chain A; UniProt 182–354 Chain F; UniProt 4–57 Chain F; UniProt 182–354 Mutation:G42D,E43N,A227D,G230D,I332A,V335I C-X-C motif chemokine 5 × 2 (P42830) C-X-C chemokine receptor type 2 × 2 (P25025) Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 2 (P62873) Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 2 (P59768) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.32 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.

83 other PDB entries and 83 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GNAO_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 16–69; UniProt 4–57 Author chain A; PDBConstruct 78–240; UniProt 182–354 Author chain F; PDBConstruct 16–69; UniProt 4–57 Author chain F; PDBConstruct 78–240; UniProt 182–354

Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1

Homo sapiens

UniProt P62873

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain E; UniProt 3–340 Chain H; UniProt 3–340 Not recorded C-X-C motif chemokine 5 × 2 (P42830) C-X-C chemokine receptor type 2 × 2 (P25025) Guanine nucleotide-binding protein G(o) subunit alpha × 2 (P09471) Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 2 (P59768) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.32 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.

1260 other PDB entries and 1263 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBB1_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain E; PDBConstruct 13–350; UniProt 3–340 Author chain H; PDBConstruct 13–350; UniProt 3–340

Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2

Homo sapiens

UniProt P59768

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain G; UniProt 1–71 Chain I; UniProt 1–71 Not recorded C-X-C motif chemokine 5 × 2 (P42830) C-X-C chemokine receptor type 2 × 2 (P25025) Guanine nucleotide-binding protein G(o) subunit alpha × 2 (P09471) Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 2 (P62873) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.32 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.

1233 other PDB entries and 1236 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBG2_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain G; PDBConstruct 1–71; UniProt 1–71 Author chain I; PDBConstruct 1–71; UniProt 1–71

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 8xx7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8xx7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8xx7
Deposition date deposition_date2024-01-17
Structure title titleStructure of CXCR2 bound to CXCL5 (CXCR2-CXCL5-Go Full 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_guinier70.42
Radius of gyration Rg (electron density) rg_electron69.79
Forward intensity I(0) i0622460000.00
Molecular weight molecular_weight214550.0 kDa
Excluded volume excluded_volume270460 ų
Envelope volume envelope_volume484780 ų
Hydration-shell volume shell_volume59770 ų
Envelope diameter envelope_diameter210.7
Shell Rg shell_rg67.06
Envelope Rg envelope_rg65.80
Shape Rg shape_rg69.78
Total Rg total_rg69.75
Total atoms total_atoms15054
Residues n_residues1938
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 dmax195.2
Rg (real space) rg_real70.82
Rg uncertainty (real space) rg_real_error1.55
I(0) (real space) i0_real6.2240e+08
I(0) uncertainty (real space) i0_real_error1.2370e+07
Rg (reciprocal space) rg_reciprocal68.54
I(0) (reciprocal space) i0_reciprocal619600000.0000
Solution quality estimate total_estimate0.6785
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary35.5
Skewness Skewness skewness0.242
Kurtosis Kurtosis kurtosis-1.160
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha14620000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.511; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.287; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)