6dc9

Fab/epitope complex of human chimeric monoclonal antibody h4E6 targeting a phosphorylated tau epitope.

Method: X-RAY DIFFRACTION Dmax: 110.4 Å Quality: EXCELLENT

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

Microtubule-associated protein tau

OrganismNot specified

UniProt P10636

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 P; UniProt 696–725 Non-standard monomer:Yes (specific site not provided by mmCIF) Fab heavy chain × 1 Fab light chain × 1 GOL GLYCEROL × 1 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;25.5% polyethylene glycol 4000 and 0.17 M ammonium sulfate Resolution 3.00 Å R-free 0.260
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain Q; UniProt 696–725 Non-standard monomer:Yes (specific site not provided by mmCIF) Fab heavy chain × 1 Fab light chain × 1 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;25.5% polyethylene glycol 4000 and 0.17 M ammonium sulfate Resolution 3.00 Å R-free 0.260

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.

248 other PDB entries and 269 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TAU_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain P; PDBConstruct 1–30; UniProt 696–725 Author chain Q; PDBConstruct 1–30; UniProt 696–725

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 6dc9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6dc9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6dc9
Deposition date deposition_date2018-05-04
Structure title titleFab/epitope complex of human chimeric monoclonal antibody h4E6 targeting a phosphorylated tau epitope.
Keywords keywordsmonoclonal antibody, fab, tau, phosphorylation state -specific antibody, 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_guinier34.53
Radius of gyration Rg (electron density) rg_electron33.92
Forward intensity I(0) i0146106000.00
Molecular weight molecular_weight94083.0 kDa
Excluded volume excluded_volume116580 ų
Envelope volume envelope_volume154710 ų
Hydration-shell volume shell_volume38342 ų
Envelope diameter envelope_diameter109.0
Shell Rg shell_rg40.09
Envelope Rg envelope_rg33.38
Shape Rg shape_rg33.89
Total Rg total_rg34.47
Total atoms total_atoms6613
Residues n_residues862
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 dmax110.4
Rg (real space) rg_real34.50
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real1.4610e+08
I(0) uncertainty (real space) i0_real_error2.4970e+06
Rg (reciprocal space) rg_reciprocal34.52
I(0) (reciprocal space) i0_reciprocal146100000.0000
Solution quality estimate total_estimate0.9093
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary40.8
Skewness Skewness skewness0.223
Kurtosis Kurtosis kurtosis-0.643
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21490000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.954; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.964

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id6dc9H02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6dc9I02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6dc9L01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6dc9L02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6dc9M01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6dc9M02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)