3fpu

The crystallographic structure of the Complex between Evasin-1 and CCL3

Method: X-RAY DIFFRACTION Dmax: 59.9 Å Quality: GOOD

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

Evasin-1

Rhipicephalus sanguineus

UniProt P0C8E7

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 21–114 Not recorded C-C motif chemokine 3 × 1 (P10147) NI NICKEL (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.1;291 K;24% (w/v) PEG 3350, 200mM Ammonium sulfate, 100mM HEPES, pH 8.1, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 1.76 Å R-free 0.285

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.

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

View Construct and Data Evidence
UniProt name EVA1_RHISA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–94; UniProt 21–114

C-C motif chemokine 3

Homo sapiens

UniProt P10147

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 B; UniProt 24–92 Mutation:A10T Evasin-1 × 1 (P0C8E7) NI NICKEL (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.1;291 K;24% (w/v) PEG 3350, 200mM Ammonium sulfate, 100mM HEPES, pH 8.1, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 1.76 Å R-free 0.285

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.

12 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CCL3_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–70; UniProt 24–92

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 3fpu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3fpu
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3fpu
Deposition date deposition_date2009-01-06
Structure title titleThe crystallographic structure of the Complex between Evasin-1 and CCL3
Keywords keywordsprotein:protein complex, chemokine, Glycoprotein, Secreted, Chemotaxis, Cytokine, Inflammatory response, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.82
Radius of gyration Rg (electron density) rg_electron16.72
Forward intensity I(0) i07874590.00
Molecular weight molecular_weight18814.0 kDa
Excluded volume excluded_volume22768 ų
Envelope volume envelope_volume27739 ų
Hydration-shell volume shell_volume14392 ų
Envelope diameter envelope_diameter58.9
Shell Rg shell_rg22.19
Envelope Rg envelope_rg17.19
Shape Rg shape_rg16.71
Total Rg total_rg17.68
Total atoms total_atoms1310
Residues n_residues166
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

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

Maximum dimension Dmax dmax59.9
Rg (real space) rg_real17.79
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real7.8750e+06
I(0) uncertainty (real space) i0_real_error9.8960e+04
Rg (reciprocal space) rg_reciprocal17.80
I(0) (reciprocal space) i0_reciprocal7875000.0000
Solution quality estimate total_estimate0.8788
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.0
Skewness Skewness skewness0.326
Kurtosis Kurtosis kurtosis-0.276
Angular range angular_range— – 0.4450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1273000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.813; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3fpub_
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 (2 domains)

Domain ID domain_id3fpuA01
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology130 — Archaeosine Trna-guanine Transglycosylase; Chain: A, domain 4
Homologous superfamily homologous superfamily100
Domain ID domain_id3fpuB00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily40

8. Citations (3)

9. Files and Curves (10)