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1esr

CRYSTAL STRUCTURE OF HUMAN MONOCYTE CHEMOTACTIC PROTEIN-2

Method: X-RAY DIFFRACTION Dmax: 53.2 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

MONOCYTE CHEMOTACTIC PROTEIN 2

Homo sapiens

UniProt P80075

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 24–99 Mutation：Q24(PCA) AND K69Q Non-standard monomer：Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；292 K；Ammonium sulfate, Tris-HCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 2.00 Å R-free 0.320

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 1ESR Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
7S59 Crystal structure of the tick evasin EVA-P974 complexed to a chimera made of human chemokines CCL7 and CCL8 Deposited 2021-09-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain 2 24–38（15 aa）
Not recorded SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；291 K；0.1 M TRIS 8.5 pH (Buffer) 2 M (NH4)2SO4 (Precipitant)
Resolution 2.39 Å R-free 0.268
7S59 Crystal structure of the tick evasin EVA-P974 complexed to a chimera made of human chemokines CCL7 and CCL8 Deposited 2021-09-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain 4 24–38（15 aa）
Not recorded SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；291 K；0.1 M TRIS 8.5 pH (Buffer) 2 M (NH4)2SO4 (Precipitant)
Resolution 2.39 Å R-free 0.268
7S5A Crystal structure of human chemokine CCL8 Deposited 2021-09-10 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 24–99（76 aa）
Chain B 24–99（76 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.2 M Ammonium phosphate dibasic 20% w/v Polyethylene glycol 3,350 pH 8
Resolution 1.37 Å R-free 0.189

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

View Construct and Data Evidence
UniProt name CCL8_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–76； UniProt 24–99

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 1esr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1esr
Deposition date deposition_date2000-04-10
Structure title titleCRYSTAL STRUCTURE OF HUMAN MONOCYTE CHEMOTACTIC PROTEIN-2
Keywords keywordsCYTOKINE, CHEMOKINE, MONOCYTE CHEMOATTRACTANT PROTEIN, HIV-1, PYROGLUTAMIC ACID; CYTOKINE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier15.14 Å
Radius of gyration Rg (electron density) rg_electron14.23 Å
Forward intensity I(0) i01760640.00
Molecular weight molecular_weight8902.0 kDa
Excluded volume excluded_volume11172 ų
Envelope volume envelope_volume13604 ų
Hydration-shell volume shell_volume9040 ų
Envelope diameter envelope_diameter50.8 Å
Shell Rg shell_rg18.49 Å
Envelope Rg envelope_rg14.73 Å
Shape Rg shape_rg14.25 Å
Total Rg total_rg15.24 Å
Total atoms total_atoms623
Residues n_residues75
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 dmax53.2 Å
Rg (real space) rg_real15.21 Å
Rg uncertainty (real space) rg_real_error0.45 Å
I(0) (real space) i0_real1.7610e+06
I(0) uncertainty (real space) i0_real_error2.1120e+04
Rg (reciprocal space) rg_reciprocal15.20 Å
I(0) (reciprocal space) i0_reciprocal1761000.0000
Solution quality estimate total_estimate0.8496
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.5 Å
Skewness Skewness skewness0.459
Kurtosis Kurtosis kurtosis-0.118
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha244200.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.755; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.856; Smooth: 0.920
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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) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1esra_
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_id1esrA00
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)