4xxd

Crystal Structure of mid-region amyloid beta capture by solanezumab

Method: X-RAY DIFFRACTION Dmax: 105.8 Å Quality: EXCELLENT

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

Amyloid-beta fragment

OrganismNot specified

UniProt P05067

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 683–699 Fragment:UNP residues 683-699 Fab Light Chain × 1 Fab Heavy Chain × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4;292 K;PEG 3350, sodium citrate Resolution 2.41 Å R-free 0.290
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 683–699 Fragment:UNP residues 683-699 Fab Light Chain × 1 Fab Heavy Chain × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4;292 K;PEG 3350, sodium citrate Resolution 2.41 Å R-free 0.290

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.

211 other PDB entries and 281 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A4_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–17; UniProt 683–699 Author chain F; PDBConstruct 1–17; UniProt 683–699

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 4xxd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4xxd
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4xxd
Deposition date deposition_date2015-01-30
Structure title titleCrystal Structure of mid-region amyloid beta capture by solanezumab
Keywords keywordsFab, Amyloid-beta, 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_guinier33.61
Radius of gyration Rg (electron density) rg_electron32.90
Forward intensity I(0) i0137912000.00
Molecular weight molecular_weight93333.0 kDa
Excluded volume excluded_volume116650 ų
Envelope volume envelope_volume155110 ų
Hydration-shell volume shell_volume39586 ų
Envelope diameter envelope_diameter103.9
Shell Rg shell_rg39.63
Envelope Rg envelope_rg32.41
Shape Rg shape_rg32.89
Total Rg total_rg33.50
Total atoms total_atoms6576
Residues n_residues849
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 dmax105.8
Rg (real space) rg_real33.52
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real1.3790e+08
I(0) uncertainty (real space) i0_real_error2.0420e+06
Rg (reciprocal space) rg_reciprocal33.57
I(0) (reciprocal space) i0_reciprocal137900000.0000
Solution quality estimate total_estimate0.9106
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary42.8
Skewness Skewness skewness0.164
Kurtosis Kurtosis kurtosis-0.607
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha18980000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.959; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.960

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id4xxdA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4xxdA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4xxdB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4xxdB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4xxdD01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4xxdD02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4xxdE01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4xxdE02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)