5o4o

HER3 in complex with Fab MF3178

Method: X-RAY DIFFRACTION Dmax: 148.8 Å Quality: REASONABLE

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

Receptor tyrosine-protein kinase erbB-3

Homo sapiens

UniProt P21860

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 3 其他Polymer 2 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–643 Not recorded MF3178 FAB light chain × 1 MF3178 FAB heavy chain × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.1 M bis tris propane pH 8.5, 0.2 M potassium thyocianate and 20% w/v PEG 3350 Resolution 3.40 Å R-free 0.261

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.

22 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ERBB3_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–643; UniProt 1–643

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 5o4o

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5o4o
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5o4o
Deposition date deposition_date2017-05-30
Structure title titleHER3 in complex with Fab MF3178
Keywords keywordsHER3 ectodomain, complex, Fab, 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_guinier40.89
Radius of gyration Rg (electron density) rg_electron41.19
Forward intensity I(0) i0125170000.00
Molecular weight molecular_weight86509.0 kDa
Excluded volume excluded_volume106820 ų
Envelope volume envelope_volume161380 ų
Hydration-shell volume shell_volume36089 ų
Envelope diameter envelope_diameter152.4
Shell Rg shell_rg40.93
Envelope Rg envelope_rg41.41
Shape Rg shape_rg41.11
Total Rg total_rg41.40
Total atoms total_atoms6065
Residues n_residues776
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 dmax148.8
Rg (real space) rg_real41.40
Rg uncertainty (real space) rg_real_error2.13
I(0) (real space) i0_real1.2520e+08
I(0) uncertainty (real space) i0_real_error2.6360e+06
Rg (reciprocal space) rg_reciprocal40.90
I(0) (reciprocal space) i0_reciprocal125100000.0000
Solution quality estimate total_estimate0.7466
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary34.4
Skewness Skewness skewness0.607
Kurtosis Kurtosis kurtosis-0.290
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7247000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.549; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.350; Smooth: 0.704

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id5o4oA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5o4oA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5o4oB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)