3l15

Human Tead2 transcriptional factor

Method: X-RAY DIFFRACTION Dmax: 72.6 Å Quality: EXCELLENT

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

Transcriptional enhancer factor TEF-4

Homo sapiens

UniProt Q15562

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 217–447 Fragment:C-terminal residues 217-447 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.4;293 K;0.1 M Tris, 2.5 M Sodium Formate, 100 mM NaCl, 2 mM MgCl2, 1 mM TCEP, 5% (w/v) Glycerol;, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.00 Å R-free 0.244
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 217–447 Fragment:C-terminal residues 217-447 Non-standard monomer:Yes (specific site not provided by mmCIF) GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.4;293 K;0.1 M Tris, 2.5 M Sodium Formate, 100 mM NaCl, 2 mM MgCl2, 1 mM TCEP, 5% (w/v) Glycerol;, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.00 Å R-free 0.244

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.

41 other PDB entries and 78 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TEAD2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–231; UniProt 217–447 Author chain B; PDBConstruct 1–231; UniProt 217–447

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 3l15

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3l15
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3l15
Deposition date deposition_date2009-12-10
Structure title titleHuman Tead2 transcriptional factor
Keywords keywordsActivator, DNA-binding, Nucleus, Transcription, Transcription regulation; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.64
Radius of gyration Rg (electron density) rg_electron22.31
Forward intensity I(0) i037302100.00
Molecular weight molecular_weight47090.0 kDa
Excluded volume excluded_volume58853 ų
Envelope volume envelope_volume70607 ų
Hydration-shell volume shell_volume26156 ų
Envelope diameter envelope_diameter73.9
Shell Rg shell_rg29.41
Envelope Rg envelope_rg22.32
Shape Rg shape_rg22.31
Total Rg total_rg23.18
Total atoms total_atoms6533
Residues n_residues389
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 dmax72.6
Rg (real space) rg_real23.50
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real3.7300e+07
I(0) uncertainty (real space) i0_real_error5.1340e+05
Rg (reciprocal space) rg_reciprocal23.54
I(0) (reciprocal space) i0_reciprocal37300000.0000
Solution quality estimate total_estimate0.9075
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.5
Skewness Skewness skewness0.156
Kurtosis Kurtosis kurtosis-0.475
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5735000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.936; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3l15a_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.18 — E set domains
Family Family familyb.1.18.26 — TEAD-like transcription factors, E-set domain
Domain ID domain_idd3l15b_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.18 — E set domains
Family Family familyb.1.18.26 — TEAD-like transcription factors, E-set domain

CATH v4.4 (2 domains)

Domain ID domain_id3l15A00
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology50 — Coagulation Factor XIII; Chain A, domain 1
Homologous superfamily homologous superfamily80
Domain ID domain_id3l15B00
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology50 — Coagulation Factor XIII; Chain A, domain 1
Homologous superfamily homologous superfamily80

8. Citations (4)

9. Files and Curves (10)