1ji7

Crystal Structure of TEL SAM Polymer

Method: X-RAY DIFFRACTION Dmax: 76.4 Å Quality: GOOD

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

ETS-RELATED PROTEIN TEL1

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 Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 47–123 Chain B; UniProt 47–123 Chain C; UniProt 47–123 Fragment:TEL SAM domain Non-standard monomer:Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;298 K;Li2SO4, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.45 Å R-free 0.195

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 1–77; UniProt 47–123 Author chain B; PDBConstruct 1–77; UniProt 47–123 Author chain C; PDBConstruct 1–77; UniProt 47–123

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 1ji7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1ji7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1ji7
Deposition date deposition_date2001-06-29
Structure title titleCrystal Structure of TEL SAM Polymer
Keywords keywordsHelical polymer, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.54
Radius of gyration Rg (electron density) rg_electron21.57
Forward intensity I(0) i015582000.00
Molecular weight molecular_weight29160.0 kDa
Excluded volume excluded_volume36099 ų
Envelope volume envelope_volume43943 ų
Hydration-shell volume shell_volume17961 ų
Envelope diameter envelope_diameter78.0
Shell Rg shell_rg27.12
Envelope Rg envelope_rg21.76
Shape Rg shape_rg21.57
Total Rg total_rg22.34
Total atoms total_atoms2051
Residues n_residues236
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 dmax76.4
Rg (real space) rg_real22.63
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real1.5580e+07
I(0) uncertainty (real space) i0_real_error2.1910e+05
Rg (reciprocal space) rg_reciprocal22.61
I(0) (reciprocal space) i0_reciprocal15580000.0000
Solution quality estimate total_estimate0.8688
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.0
Skewness Skewness skewness0.428
Kurtosis Kurtosis kurtosis-0.395
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3502000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.795; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.908; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1ji7a_
Class classa — All alpha proteins
Fold Fold folda.60 — SAM domain-like
Superfamily Superfamily superfamilya.60.1 — SAM/Pointed domain
Family Family familya.60.1.1 — Pointed domain
Domain ID domain_idd1ji7b_
Class classa — All alpha proteins
Fold Fold folda.60 — SAM domain-like
Superfamily Superfamily superfamilya.60.1 — SAM/Pointed domain
Family Family familya.60.1.1 — Pointed domain
Domain ID domain_idd1ji7c1
Class classa — All alpha proteins
Fold Fold folda.60 — SAM domain-like
Superfamily Superfamily superfamilya.60.1 — SAM/Pointed domain
Family Family familya.60.1.1 — Pointed domain
Domain ID domain_idd1ji7c2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (3 domains)

Domain ID domain_id1ji7A00
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_id1ji7B00
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_id1ji7C00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily50 — Transcription Factor, Ets-1

8. Citations (1)

9. Files and Curves (10)