SAXSdb — 8xvu

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

C-X-C chemokine receptor type 2

Homo sapiens

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain R； UniProt 2–360	Not recorded	C-X-C motif chemokine 2 × 2 （P19875）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.09 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.

Other PDB	Difference from Current Entry 8XVU	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
4MPA Crystal structure of NHERF1-CXCR2 signaling complex in P21 space group Deposited 2013-09-12	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 356–360（5 aa） Fragment：SEE REMARK 999	Not recorded	ACY ACETIC ACID × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.8；293 K；100 mM sodium acetate, pH 4.8, 0.2 M ammonium acetate, 24% PEG4000, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.10 Å R-free 0.157
4Q3H The crystal structure of NHERF1 PDZ2 CXCR2 complex revealed by the NHERF1 CXCR2 chimeric protein Deposited 2014-04-11	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 356–360（5 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；100 mM Tris HCl, pH 8.5, 8% PEG8000, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.44 Å R-free 0.195
4Q3H The crystal structure of NHERF1 PDZ2 CXCR2 complex revealed by the NHERF1 CXCR2 chimeric protein Deposited 2014-04-11	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain B 356–360（5 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；100 mM Tris HCl, pH 8.5, 8% PEG8000, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.44 Å R-free 0.195
5TYT Crystal Structure of the PDZ domain of RhoGEF bound to CXCR2 C-terminal peptide Deposited 2016-11-21	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 356–360（5 aa） Fragment：Rho (UNP residues 41-123), CXCR2 C-terminal peptide (UNP residues 356-360) Chain B 356–360（5 aa） Fragment：Rho (UNP residues 41-123), CXCR2 C-terminal peptide (UNP residues 356-360)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；293 K；25% PEG8000, 0.1 M sodium citrate, 0.2 M sodium acetate	Resolution 2.40 Å R-free 0.240
5TYT Crystal Structure of the PDZ domain of RhoGEF bound to CXCR2 C-terminal peptide Deposited 2016-11-21	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 356–360（5 aa） Fragment：Rho (UNP residues 41-123), CXCR2 C-terminal peptide (UNP residues 356-360) Chain D 356–360（5 aa） Fragment：Rho (UNP residues 41-123), CXCR2 C-terminal peptide (UNP residues 356-360)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；293 K；25% PEG8000, 0.1 M sodium citrate, 0.2 M sodium acetate	Resolution 2.40 Å R-free 0.240
6KVA Structure of anti-hCXCR2 abN48-2 in complex with its CXCR2 epitope Deposited 2019-09-03	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 9–19（11 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；0.1M HEPES pH 7.5, 25% w/v Polyethylene glycol 3350	Resolution 2.20 Å R-free 0.234
6KVA Structure of anti-hCXCR2 abN48-2 in complex with its CXCR2 epitope Deposited 2019-09-03	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain b 9–19（11 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；0.1M HEPES pH 7.5, 25% w/v Polyethylene glycol 3350	Resolution 2.20 Å R-free 0.234
6KVF Structure of anti-hCXCR2 abN48 in complex with its CXCR2 epitope Deposited 2019-09-04	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain b 9–19（11 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；0.1M HEPES sodium pH 7.5, 2% v/v Polyethylene glycol 400, 2.0M Ammonium sulfate	Resolution 2.79 Å R-free 0.264
6KVF Structure of anti-hCXCR2 abN48 in complex with its CXCR2 epitope Deposited 2019-09-04	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 9–19（11 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；0.1M HEPES sodium pH 7.5, 2% v/v Polyethylene glycol 400, 2.0M Ammonium sulfate	Resolution 2.79 Å R-free 0.264
6LFL Crystal structure of a class A GPCR Deposited 2019-12-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 37–241（205 aa） Chain A 244–344（101 aa）	Mutation：L135W, A249E, G303A Mutation：L135W, A249E, G303A	EBX 4-[[3,4-bis(oxidanylidene)-2-[[(1~{R})-1-(4-propan-2-ylfuran-2-yl)propyl]amino]cyclobuten-1-yl]amino]-~{N},~{N}-dimethyl-3-oxidanyl-pyridine-2-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions LIPIDIC CUBIC PHASE；293 K；100mM HEPES pH7.0, 32% PEG 400, 50-150 mM Sodium tartrate dibasic dihydrate salt	Resolution 3.20 Å R-free 0.264
6LFM Cryo-EM structure of a class A GPCR Deposited 2019-12-03	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain R 1–360（360 aa）	Not recorded	CLR CHOLESTEROL × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
6LFO Cryo-EM structure of a class A GPCR monomer Deposited 2019-12-03	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain R 1–360（360 aa）	Not recorded	CLR CHOLESTEROL × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
8XWA Structure of CXCR2 bound to CXCL1 (Ligand-receptor focused map) Deposited 2024-01-16	Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain R 2–360（359 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.48 Å
8XWF Structure of CXCR2 bound to CXCL3 (Ligand-receptor focused map) Deposited 2024-01-16	Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain R 2–360（359 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.65 Å
8XWM Structure of CXCR2 bound to CXCL6 (Ligand-receptor focused map) Deposited 2024-01-16	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain R 2–360（359 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.71 Å
8XWN Structure of CXCR2 bound to CXCL8 (Ligand-receptor focused map) Deposited 2024-01-16	Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain R 2–360（359 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.29 Å
8XWS Structure of CXCR2 bound to CXCL5 (Ligand-receptor focused map) Deposited 2024-01-16	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 2–360（359 aa） Chain R 2–360（359 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.06 Å
8XWV Structure of CXCR2 bound to CXCL1 (CXCR2-CXCL1-Go Full map) Deposited 2024-01-16	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain R 2–360（359 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.07 Å
8XX3 Structure of CXCR2 bound to CXCL3 (CXCR2-CXCL3-Go Full map) Deposited 2024-01-17	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain R 2–360（359 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.38 Å
8XX6 Structure of CXCR2 bound to CXCL8 (CXCR2-CXCL8-Go Full map) Deposited 2024-01-17	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain R 2–360（359 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.99 Å
8XX7 Structure of CXCR2 bound to CXCL5 (CXCR2-CXCL5-Go Full map) Deposited 2024-01-17	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain C 2–360（359 aa） Chain R 2–360（359 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.32 Å
8XXH Structure of CXCR2 bound to CXCL2 (CXCR2-CXCL2-Go Full map) Deposited 2024-01-18	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain R 2–360（359 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å
8XXR Structure of CXCR2 bound to CXCL6 (CXCR2-CXCL6-Go Full map) Deposited 2024-01-18	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain R 2–360（359 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.17 Å
8XXX Structure of CXCR2 bound to CXCL6 (Composite map) Deposited 2024-01-19	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain R 2–360（359 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.17 Å

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	1
Chains and sequence ranges	Author chain R； PDBConstruct 58–416； UniProt 2–360

C-X-C motif chemokine 2

Homo sapiens

UniProt P19875

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain D； UniProt 35–107 Chain E； UniProt 35–107	Not recorded	C-X-C chemokine receptor type 2 × 1 （P25025）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.09 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.

Other PDB	Difference from Current Entry 8XVU	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1QNK TRUNCATED HUMAN GROB[5-73], NMR, 20 STRUCTURES Deposited 1999-10-18	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 39–107（69 aa） Fragment：Residues 5-73 Chain B 39–107（69 aa） Fragment：Residues 5-73	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；303 K；Pressure 1 NMR sample composition 90%H2O/10%D2O	Resolution not provided
5OB5 fAb complex with GroBeta. AbVance: increasing our knowledge of antibody structural space to enable faster and better decision-making in antibody drug discovery. Deposited 2017-06-26	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 40–102（63 aa）	Not recorded	GOL GLYCEROL × 4 SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；293 K；1.6M ammonium sulfate, 0.5M lithium chloride. 5-30% glycerol added as cryoprotectant	Resolution 1.65 Å R-free 0.195
8XXH Structure of CXCR2 bound to CXCL2 (CXCR2-CXCL2-Go Full map) Deposited 2024-01-18	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain D 35–107（73 aa） Chain E 35–107（73 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CXCL2_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain D； PDBConstruct 1–73； UniProt 35–107 Author chain E； PDBConstruct 1–73； UniProt 35–107

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	8xvu
Deposition date deposition_date	2024-01-15
Structure title title	Structure of CXCR2 bound to CXCL2 (Ligand-receptor focused map)
Keywords keywords	GPCR, Arrestin, SIGNALING PROTEIN-IMMUNE SYSTEM complex; SIGNALING PROTEIN/IMMUNE SYSTEM
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	27.49 Å
Radius of gyration Rg (electron density) rg_electron	27.09 Å
Forward intensity I(0) i0	31626000.00
Molecular weight molecular_weight	46876.0 kDa
Excluded volume excluded_volume	60331 Å³
Envelope volume envelope_volume	75916 Å³
Hydration-shell volume shell_volume	25352 Å³
Envelope diameter envelope_diameter	96.6 Å
Shell Rg shell_rg	32.35 Å
Envelope Rg envelope_rg	27.50 Å
Shape Rg shape_rg	27.07 Å
Total Rg total_rg	27.83 Å
Total atoms total_atoms	3288
Residues n_residues	427
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	92.7 Å
Rg (real space) rg_real	27.87 Å
Rg uncertainty (real space) rg_real_error	0.93 Å
I(0) (real space) i0_real	3.1630e+07
I(0) uncertainty (real space) i0_real_error	5.3810e+05
Rg (reciprocal space) rg_reciprocal	27.76 Å
I(0) (reciprocal space) i0_reciprocal	31620000.0000
Solution quality estimate total_estimate	0.8158
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	25.6 Å
Skewness Skewness skewness	0.626
Kurtosis Kurtosis kurtosis	-0.230
Angular range angular_range	— – 0.2900 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	7927000.0000
Real-space data points n_real_points	59
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.677; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.752; Smooth: 0.827

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	C-X-C chemokine receptor type 2
Molecular weight formula_weight	46699.6 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	R
Atom count atom_count	3288

MGKTIIALSYIFCLVFADYKDDDDAANFTPVNGSSGNQSVRLVTSSSLEVLFQGPGSEDFNMESDSFEDFWKGEDLSNYSYSSTLPPFLLDAAPCEPESLEINKYFVVIIYALVFLLSLLGNSLVMLVILYSRVGRSVTDVYLLNLALADLLFALTLPIWAASKVNGWIFGTFLCKVVSLLKEVNFYSGILLLACISVDRYLAIVHATRTLTQKRYLVKFICLSIWGLSLLLALPVLLFRRTVYSSNVSPACYEDMGNNTANWRMLLRILPQSFGFIVPLLIMLFCYGFTLRTLFKAHMGQKHRAMRVIFAVVLIFLLCWLPYNLVLLADTLMRTQVIQETCERRNHIDRALDATEILGILHSCLNPLIYAFIGQKFRHGLLKILAIHGLISKDSLPKDSRPSFVGSSSGHTSTTL

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Spodoptera frugiperda

Entity 2 Entity 2 polymer

Description description	C-X-C motif chemokine 2
Molecular weight formula_weight	7905.4 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,E

APLATELRCQCLQTLQGIHLKNIQSVKVKSPGPHCAQTEVIATLKNGQKACLNPASPMVKKIIEKMLKNGKSN

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	—

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	3.09 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	285884

fit	/app/data/saxs_computation/xv/8xvu/8xvu.fit
pddf	/app/data/pr_computation/xv/8xvu/8xvu.pr.out
profile	/app/data/saxs_computation/xv/8xvu/8xvu.dat

Structure of CXCR2 bound to CXCL2 (Ligand-receptor focused map)

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

C-X-C chemokine receptor type 2

State in the Current Structure

Other States of the Same Protein in the Database

C-X-C motif chemokine 2

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)