2gy5

Tie2 Ligand-Binding Domain Crystal Structure

Method: X-RAY DIFFRACTION Dmax: 89.0 Å Quality: GOOD

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

Angiopoietin-1 receptor

Homo sapiens

UniProt Q02763

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 23–445 Fragment:Ligand-binding domain (residues 23-445) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NDG 2-acetamido-2-deoxy-alpha-D-glucopyranose × 4 SO4 SULFATE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;2.2M Ammonium Sulfate, 0.1M MES, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.90 Å R-free 0.294

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.

15 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TIE2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–423; UniProt 23–445

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 2gy5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2gy5
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2gy5
Deposition date deposition_date2006-05-09
Structure title titleTie2 Ligand-Binding Domain Crystal Structure
Keywords keywordsligand-binding domain, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.35
Radius of gyration Rg (electron density) rg_electron23.84
Forward intensity I(0) i043723300.00
Molecular weight molecular_weight48580.0 kDa
Excluded volume excluded_volume59820 ų
Envelope volume envelope_volume74369 ų
Hydration-shell volume shell_volume26488 ų
Envelope diameter envelope_diameter92.4
Shell Rg shell_rg30.48
Envelope Rg envelope_rg24.07
Shape Rg shape_rg23.89
Total Rg total_rg24.47
Total atoms total_atoms3383
Residues n_residues423
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 dmax89.0
Rg (real space) rg_real24.34
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real4.3720e+07
I(0) uncertainty (real space) i0_real_error6.2570e+05
Rg (reciprocal space) rg_reciprocal24.35
I(0) (reciprocal space) i0_reciprocal43720000.0000
Solution quality estimate total_estimate0.8365
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.7
Skewness Skewness skewness0.393
Kurtosis Kurtosis kurtosis-0.083
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha6233000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.653; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.910; Smooth: 1.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id2gy5A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2gy5A02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2gy5A03
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology300 — Tie2 ligand-binding domain fold
Homologous superfamily homologous superfamily10 — Tie2 ligand-binding domain superfamily
Domain ID domain_id2gy5A04
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)