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1lv9

CXCR3 Binding Chemokine IP-10/CXCL10

Method: SOLUTION NMR Dmax: 39.7 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Small inducible cytokine B10

OrganismNot specified

UniProt P02778

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 22–98 Non-standard monomer：Yes (specific site not provided by mmCIF) No other associated polymer 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

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 1LV9 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
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 method 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
1O7Z Crystal structure of IP-10 T-form Deposited 2002-11-20 Different construct Different mutation/modification 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 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 1.92 Å R-free 0.298
1O80 Crystal structure of IP-10 H-Form Deposited 2002-11-20 Different construct Different mutation/modification 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 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 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 SCYBA_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； 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.

SAXS scattering curve SAXS Profile

SAXS profile for 1lv9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1lv9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1lv9
Deposition date deposition_date2002-05-27
Structure title titleCXCR3 Binding Chemokine IP-10/CXCL10
Keywords keywordschemokine, CYTOKINE; CYTOKINE
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier10.99 Å
Radius of gyration Rg (electron density) rg_electron11.08 Å
Forward intensity I(0) i069979300.00
Molecular weight molecular_weight71577.0 kDa
Excluded volume excluded_volume91101 ų
Envelope volume envelope_volume14707 ų
Hydration-shell volume shell_volume10119 ų
Envelope diameter envelope_diameter43.0 Å
Shell Rg shell_rg18.06 Å
Envelope Rg envelope_rg12.93 Å
Shape Rg shape_rg11.06 Å
Total Rg total_rg11.49 Å
Total atoms total_atoms10290
Residues n_residues630
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax39.7 Å
Rg (real space) rg_real10.96 Å
Rg uncertainty (real space) rg_real_error0.24 Å
I(0) (real space) i0_real6.9980e+07
I(0) uncertainty (real space) i0_real_error6.7660e+05
Rg (reciprocal space) rg_reciprocal10.96 Å
I(0) (reciprocal space) i0_reciprocal69980000.0000
Solution quality estimate total_estimate0.8296
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary13.6 Å
Skewness Skewness skewness0.257
Kurtosis Kurtosis kurtosis-0.095
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha85880.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.604; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.995
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1lv9a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.9 — IL8-like
Superfamily Superfamily superfamilyd.9.1 — Interleukin 8-like chemokines
Family Family familyd.9.1.1 — Interleukin 8-like chemokines

CATH v4.4 (1 domains)

Domain ID domain_id1lv9A00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily40 —
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8. Citations (1)

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9. Files and Curves (10)