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2mpm

Structural Basis of Receptor Sulfotyrosine Recognition by a CC Chemokine: the N-terminal Region of CCR3 Bound to CCL11/Eotaxin-1

Method: SOLUTION NMR Dmax: 47.1 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Eotaxin

Homo sapiens

UniProt P51671

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 24–97 Not recorded CCR3 × 1 SOLUTION NMR NMR measurement conditions：pH 6.5；313 K；Ionic strength (raw mmCIF value) 20；Pressure AMBIENT NMR sample composition：0.2-0.4 MM [U-100% 13C, U-100% 15N] CCL11/EOTAXIN-1, 0.2-0.4 MM CCR3 SU1617 SULFOPEPTIDE, 95% V/V H2O, 5% V/V [U-100% 2H] D2O, 20 MM [U-100% 2H] SODIUM ACETATE-D6, 0.02% V/V SODIUM AZIDE, 20 UM DSS, 95% H2O/5% 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 2MPM Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1EOT SOLUTION NMR STRUCTURE OF EOTAXIN, MINIMIZED AVERAGE STRUCTURE Deposited 1998-06-17 Different oligomeric state Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 24–97（74 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5；303 K；Ionic strength (raw mmCIF value) 20mM SODIUM ACETATE；Pressure 1
NMR sample composition 90% H2O/10% H2O OR 100% D2O. BUFFER ALSO CONTAINED 1MM DSS AND 1MM SODIUM AZIDE.
Resolution not provided
2EOT SOLUTION STRUCTURE OF EOTAXIN, AN ENSEMBLE OF 32 NMR SOLUTION STRUCTURES Deposited 1998-06-29 Different oligomeric state Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 24–97（74 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5；303 K；Ionic strength (raw mmCIF value) 20mM SODIUM ACETATE；Pressure 1
NMR sample composition 90% H2O/10% H2O OR 100% D2O BUFFER, ALSO CONTAINED 1MM DSS AND 1MM SODIUM AZIDE
Resolution not provided
7SCS Crystal Structure of the Tick Evasin EVA-AAM1001 Complexed to Human Chemokine CCL11 Deposited 2021-09-29 Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 24–97（74 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.1 M BIS-TRIS 6.5 pH (Buffer) , 2 M (NH4)2SO4 (Precipitant)
Resolution 1.51 Å R-free 0.206

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

View Construct and Data Evidence
UniProt name CCL11_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–74； UniProt 24–97

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 2mpm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2mpm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2mpm
Deposition date deposition_date2014-05-26
Structure title titleStructural Basis of Receptor Sulfotyrosine Recognition by a CC Chemokine: the N-terminal Region of CCR3 Bound to CCL11/Eotaxin-1
Keywords keywordsChemokine CCL11, Chemokine Receptor CCR3, Sulfopeptide, 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_guinier13.32 Å
Radius of gyration Rg (electron density) rg_electron13.14 Å
Forward intensity I(0) i0586964000.00
Molecular weight molecular_weight206300.0 kDa
Excluded volume excluded_volume259280 ų
Envelope volume envelope_volume28992 ų
Hydration-shell volume shell_volume15345 ų
Envelope diameter envelope_diameter53.0 Å
Shell Rg shell_rg21.82 Å
Envelope Rg envelope_rg16.13 Å
Shape Rg shape_rg13.13 Å
Total Rg total_rg13.38 Å
Total atoms total_atoms29040
Residues n_residues1760
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 dmax47.1 Å
Rg (real space) rg_real13.23 Å
Rg uncertainty (real space) rg_real_error0.43 Å
I(0) (real space) i0_real5.8700e+08
I(0) uncertainty (real space) i0_real_error6.7860e+06
Rg (reciprocal space) rg_reciprocal13.23 Å
I(0) (reciprocal space) i0_reciprocal587000000.0000
Solution quality estimate total_estimate0.8521
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.5 Å
Skewness Skewness skewness0.103
Kurtosis Kurtosis kurtosis-0.421
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha319400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.700; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.991
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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) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2mpmA00
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)