2ypa

Structure of the SCL:E47:LMO2:LDB1 complex bound to DNA

Method: X-RAY DIFFRACTION Dmax: 88.2 Å Quality: GOOD

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

T-CELL ACUTE LYMPHOCYTIC LEUKEMIA PROTEIN 1

HOMO SAPIENS

UniProt P17542

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–DNA Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain A; UniProt 180–253 Fragment:BHLH, RESIDUES 180-253 TRANSCRIPTION FACTOR E2-ALPHA × 1 (P15923) RHOMBOTIN-2 × 1 (P25791) LIM DOMAIN-BINDING PROTEIN 1 × 1 (Q86U70) EBOX FORWARD × 1 EBOX REVERSE × 1 ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;5 % (V/V) 2-METHYL-2, 4-PENTANEDIOL (MPD), 40 MM MAGNESIUM CHLORIDE, 50 MM SODIUM CACODYLATE PH 6.0 AND 2MM GLUTATHIONE Resolution 2.80 Å R-free 0.269

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TAL1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 18–91; UniProt 180–253

TRANSCRIPTION FACTOR E2-ALPHA

HOMO SAPIENS

UniProt P15923

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–DNA Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain B; UniProt 535–613 Fragment:RESIDUES 535-613 T-CELL ACUTE LYMPHOCYTIC LEUKEMIA PROTEIN 1 × 1 (P17542) RHOMBOTIN-2 × 1 (P25791) LIM DOMAIN-BINDING PROTEIN 1 × 1 (Q86U70) EBOX FORWARD × 1 EBOX REVERSE × 1 ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;5 % (V/V) 2-METHYL-2, 4-PENTANEDIOL (MPD), 40 MM MAGNESIUM CHLORIDE, 50 MM SODIUM CACODYLATE PH 6.0 AND 2MM GLUTATHIONE Resolution 2.80 Å R-free 0.269

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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TFE2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–82; UniProt 535–613

RHOMBOTIN-2

HOMO SAPIENS

UniProt P25791

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–DNA Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain C; UniProt 25–156 Fragment:LIM, RESIDUES 25-156 T-CELL ACUTE LYMPHOCYTIC LEUKEMIA PROTEIN 1 × 1 (P17542) TRANSCRIPTION FACTOR E2-ALPHA × 1 (P15923) LIM DOMAIN-BINDING PROTEIN 1 × 1 (Q86U70) EBOX FORWARD × 1 EBOX REVERSE × 1 ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;5 % (V/V) 2-METHYL-2, 4-PENTANEDIOL (MPD), 40 MM MAGNESIUM CHLORIDE, 50 MM SODIUM CACODYLATE PH 6.0 AND 2MM GLUTATHIONE Resolution 2.80 Å R-free 0.269

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.

3 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBTN2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 14–145; UniProt 25–156

LIM DOMAIN-BINDING PROTEIN 1

HOMO SAPIENS

UniProt Q86U70

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–DNA Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain D; UniProt 336–375 Fragment:LID, RESIDUES 336-375 T-CELL ACUTE LYMPHOCYTIC LEUKEMIA PROTEIN 1 × 1 (P17542) TRANSCRIPTION FACTOR E2-ALPHA × 1 (P15923) RHOMBOTIN-2 × 1 (P25791) EBOX FORWARD × 1 EBOX REVERSE × 1 ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;5 % (V/V) 2-METHYL-2, 4-PENTANEDIOL (MPD), 40 MM MAGNESIUM CHLORIDE, 50 MM SODIUM CACODYLATE PH 6.0 AND 2MM GLUTATHIONE Resolution 2.80 Å R-free 0.269

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.

8 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LDB1_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 12–51; UniProt 336–375

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 2ypa

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2ypa
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2ypa
Deposition date deposition_date2012-10-30
Structure title titleStructure of the SCL:E47:LMO2:LDB1 complex bound to DNA
Keywords keywordsIMMUNE SYSTEM, HEMATOPOIESIS, LEUKEMIA; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.06
Radius of gyration Rg (electron density) rg_electron26.40
Forward intensity I(0) i038666900.00
Molecular weight molecular_weight41971.0 kDa
Excluded volume excluded_volume49968 ų
Envelope volume envelope_volume70025 ų
Hydration-shell volume shell_volume23155 ų
Envelope diameter envelope_diameter89.5
Shell Rg shell_rg32.23
Envelope Rg envelope_rg26.68
Shape Rg shape_rg26.40
Total Rg total_rg26.99
Total atoms total_atoms2894
Residues n_residues318
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 dmax88.2
Rg (real space) rg_real27.03
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real3.8670e+07
I(0) uncertainty (real space) i0_real_error5.9240e+05
Rg (reciprocal space) rg_reciprocal27.04
I(0) (reciprocal space) i0_reciprocal38670000.0000
Solution quality estimate total_estimate0.8909
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary23.9
Skewness Skewness skewness0.154
Kurtosis Kurtosis kurtosis-0.719
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4005000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.897; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.900; Smooth: 0.985

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id2ypaA00
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology280 — MYOD Basic-Helix-Loop-Helix Domain, subunit B
Homologous superfamily homologous superfamily10 — Helix-loop-helix DNA-binding domain
Domain ID domain_id2ypaB00
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology280 — MYOD Basic-Helix-Loop-Helix Domain, subunit B
Homologous superfamily homologous superfamily10 — Helix-loop-helix DNA-binding domain
Domain ID domain_id2ypaC01
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology110 — Cysteine Rich Protein
Homologous superfamily homologous superfamily10 — Cysteine Rich Protein
Domain ID domain_id2ypaC02
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology110 — Cysteine Rich Protein
Homologous superfamily homologous superfamily10 — Cysteine Rich Protein

8. Citations (1)

9. Files and Curves (10)