SAXSdb — 1o7z

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

SMALL INDUCIBLE CYTOKINE B10

OrganismNot specified

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 22–98 Chain B； UniProt 22–98	Not recorded	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8.75；10MG/ML PROTEIN,0.1M TRIS-HCL BUFFER, PH 8.75,3.3M SODIUM FORMATE	Resolution 1.92 Å R-free 0.298

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 1O7Z	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1LV9 CXCR3 Binding Chemokine IP-10/CXCL10 Deposited 2002-05-27	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 22–98（77 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5；298 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR sample composition 2 mM NMeLeu 27 IP-10 (no isotope labelling), 1 mM sodium azide, 1 mM DSS, 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided
1O7Y Crystal structure of IP-10 M-form Deposited 2002-11-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 22–98（77 aa） Chain B 22–98（77 aa） Chain C 22–98（77 aa） Chain D 22–98（77 aa）	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.4；10MG/ML PROTEIN, 16% PEG 4000, 0.1M SODIUM ACETATE BUFFER, PH 4.4, 0.2M AMMONIUM SULPHATE	Resolution 3.00 Å R-free 0.309
1O80 Crystal structure of IP-10 H-Form Deposited 2002-11-20	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 22–98（77 aa） Chain B 22–98（77 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.75；10MG/ML PROTEIN, 0.1M TRIS-HCL BUFFER, PH 8.75, 3.3M SODIUM FORMATE	Resolution 2.00 Å R-free 0.298
8K2X CXCR3-DNGi complex activated by CXCL10 Deposited 2023-07-14	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 Heteromer；Protein × 6 PDB declaration: hexameric	Chain L 1–98（98 aa）	Not recorded	CLR CHOLESTEROL × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
9P0L Composite map of CXCL10-CXCR3-Gi-scFv16 Deposited 2025-06-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 22–98（77 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å

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

View Construct and Data Evidence

UniProt name	SZ10_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–77； UniProt 22–98 Author chain B； PDBConstruct 1–77； UniProt 22–98

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	1o7z
Deposition date deposition_date	2002-11-20
Structure title title	Crystal structure of IP-10 T-form
Keywords keywords	CHEMOKINE, INTERFERON INDUCTION, CHEMOTAXIS, INFLAMMATORY RESPONSE; CHEMOKINE
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	15.67 Å
Radius of gyration Rg (electron density) rg_electron	14.33 Å
Forward intensity I(0) i0	3377150.00
Molecular weight molecular_weight	12800.0 kDa
Excluded volume excluded_volume	16140 Å³
Envelope volume envelope_volume	19711 Å³
Hydration-shell volume shell_volume	11852 Å³
Envelope diameter envelope_diameter	46.9 Å
Shell Rg shell_rg	19.75 Å
Envelope Rg envelope_rg	14.49 Å
Shape Rg shape_rg	14.32 Å
Total Rg total_rg	15.57 Å
Total atoms total_atoms	888
Residues n_residues	117
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	47.4 Å
Rg (real space) rg_real	15.56 Å
Rg uncertainty (real space) rg_real_error	0.28 Å
I(0) (real space) i0_real	3.3770e+06
I(0) uncertainty (real space) i0_real_error	4.1310e+04
Rg (reciprocal space) rg_reciprocal	15.57 Å
I(0) (reciprocal space) i0_reciprocal	3377000.0000
Solution quality estimate total_estimate	0.9047
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	46.2 Å
Skewness Skewness skewness	0.016
Kurtosis Kurtosis kurtosis	-0.524
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	443800.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.936; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.961

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1o7za_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.9 — IL8-like
Superfamily Superfamily superfamily	d.9.1 — Interleukin 8-like chemokines
Family Family family	d.9.1.1 — Interleukin 8-like chemokines

Domain ID domain_id	d1o7zb_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.9 — IL8-like
Superfamily Superfamily superfamily	d.9.1 — Interleukin 8-like chemokines
Family Family family	d.9.1.1 — Interleukin 8-like chemokines

CATH v4.4 (2 domains)

Domain ID domain_id	1o7zA00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	1o7zB00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	40 —

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8. Citations (1)

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Unit-cell length a length_a	59.437 Å
Unit-cell length b length_b	59.437 Å
Unit-cell length c length_c	121.708 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	16

Space group space_group	P 41 21 2
Space-group number int_tables_number	92
Crystal system crystal_system	—

Resolution resolution	1.920 Å
Low-resolution limit resolution_low	34.580 Å
R factor r_factor	0.2790
R_work r_work	0.2790
R_free r_free	0.2980

Description description	SMALL INDUCIBLE CYTOKINE B10
Molecular weight formula_weight	8637.3 kDa
Source method src_method	syn
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	930

Crystal structure of IP-10 T-form

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

SMALL INDUCIBLE CYTOKINE B10

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

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	42

fit	/app/data/saxs_computation/o7/1o7z/1o7z.fit
pddf	/app/data/pr_computation/o7/1o7z/1o7z.pr.out
profile	/app/data/saxs_computation/o7/1o7z/1o7z.dat