8ft6

The von Willebrand factor A domain of human capillary morphogenesis gene II, flexibly fused to the 1TEL crystallization chaperone, Ala-Ala linker variant, SUMO tag-free preparation.

Method: X-RAY DIFFRACTION Dmax: 74.2 Å Quality: GOOD

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

Transcription factor ETV6,Anthrax toxin receptor 2 chimera

Homo sapiens

UniProt P41212

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 47–124 Mutation:R14A,V77E,K87A,R89A,R91A,A225V CIT CITRIC ACID × 1 IOD IODIDE ION × 2 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;298 K;0.2M Ammonium citrate tribasic, 20% w/v PEG 3350 Resolution 2.62 Å R-free 0.234

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.

40 other PDB entries and 64 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ETV6_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 11–88; UniProt 47–124

Transcription factor ETV6,Anthrax toxin receptor 2 chimera

Homo sapiens

UniProt P58335

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 40–217 Mutation:R14A,V77E,K87A,R89A,R91A,A225V CIT CITRIC ACID × 1 IOD IODIDE ION × 2 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;298 K;0.2M Ammonium citrate tribasic, 20% w/v PEG 3350 Resolution 2.62 Å R-free 0.234

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.

13 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ANTR2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 89–266; UniProt 40–217

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 8ft6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ft6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ft6
Deposition date deposition_date2023-01-11
Structure title titleThe von Willebrand factor A domain of human capillary morphogenesis gene II, flexibly fused to the 1TEL crystallization chaperone, Ala-Ala linker variant, SUMO tag-free preparation.
Keywords keywordsTELSAM fusion, polymer forming crystallization chaperone, PEPTIDE BINDING PROTEIN; PEPTIDE BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.17
Radius of gyration Rg (electron density) rg_electron21.21
Forward intensity I(0) i012482200.00
Molecular weight molecular_weight26699.0 kDa
Excluded volume excluded_volume33349 ų
Envelope volume envelope_volume39532 ų
Hydration-shell volume shell_volume16971 ų
Envelope diameter envelope_diameter77.3
Shell Rg shell_rg26.09
Envelope Rg envelope_rg21.28
Shape Rg shape_rg21.12
Total Rg total_rg22.16
Total atoms total_atoms1879
Residues n_residues255
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 dmax74.2
Rg (real space) rg_real22.37
Rg uncertainty (real space) rg_real_error0.66
I(0) (real space) i0_real1.2480e+07
I(0) uncertainty (real space) i0_real_error2.0570e+05
Rg (reciprocal space) rg_reciprocal22.34
I(0) (reciprocal space) i0_reciprocal12480000.0000
Solution quality estimate total_estimate0.7624
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.0
Skewness Skewness skewness0.509
Kurtosis Kurtosis kurtosis-0.397
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2972000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.715; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.765; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id8ft6A01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily50 — Transcription Factor, Ets-1
Domain ID domain_id8ft6A02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily410 — von Willebrand factor, type A domain

8. Citations (2)

9. Files and Curves (10)