2qb0

Structure of the 2TEL crystallization module fused to T4 lysozyme with an Ala-Gly-Pro linker.

Method: X-RAY DIFFRACTION Dmax: 126.1 Å Quality: GOOD

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

Transcription factor ETV6

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 Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 47–123 Chain D; UniProt 47–123 Mutation:E80V MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.56 Å R-free 0.252
2 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 47–123 Chain C; UniProt 47–123 Mutation:E80V MN MANGANESE (II) ION × 3 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.56 Å R-free 0.252

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 63 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ETV6_HUMAN
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–77; UniProt 47–123 Author chain C; PDBConstruct 1–77; UniProt 47–123 Author chain B; PDBConstruct 1–77; UniProt 47–123 Author chain D; PDBConstruct 1–77; UniProt 47–123

Transcription factor ETV6,Endolysin

Homo sapiens

UniProt P00720

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 Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 2–162 Not recorded Transcription factor ETV6 × 1 (P41212) MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.56 Å R-free 0.252
2 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 2–162 Not recorded Transcription factor ETV6 × 1 (P41212) MN MANGANESE (II) ION × 3 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.56 Å R-free 0.252

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.

721 other PDB entries and 845 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ENLYS_BPT4
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 81–241; UniProt 2–162 Author chain D; PDBConstruct 81–241; UniProt 2–162

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 2qb0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2qb0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2qb0
Deposition date deposition_date2007-06-15
Structure title titleStructure of the 2TEL crystallization module fused to T4 lysozyme with an Ala-Gly-Pro linker.
Keywords keywordsHelical polymer, HYDROLASE REGULATOR; HYDROLASE REGULATOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier37.11
Radius of gyration Rg (electron density) rg_electron36.99
Forward intensity I(0) i085114800.00
Molecular weight molecular_weight73873.0 kDa
Excluded volume excluded_volume92639 ų
Envelope volume envelope_volume131620 ų
Hydration-shell volume shell_volume32395 ų
Envelope diameter envelope_diameter128.0
Shell Rg shell_rg39.42
Envelope Rg envelope_rg36.23
Shape Rg shape_rg37.02
Total Rg total_rg37.07
Total atoms total_atoms5202
Residues n_residues636
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 dmax126.1
Rg (real space) rg_real37.34
Rg uncertainty (real space) rg_real_error1.64
I(0) (real space) i0_real8.5110e+07
I(0) uncertainty (real space) i0_real_error1.5210e+06
Rg (reciprocal space) rg_reciprocal37.21
I(0) (reciprocal space) i0_reciprocal85100000.0000
Solution quality estimate total_estimate0.8477
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary44.0
Skewness Skewness skewness0.351
Kurtosis Kurtosis kurtosis-0.613
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6991000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.835; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.682; Smooth: 0.831

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2qb0a_
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_idd2qb0c_
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

CATH v4.4 (6 domains)

Domain ID domain_id2qb0A00
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_id2qb0B01
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_id2qb0B02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily40
Domain ID domain_id2qb0C00
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_id2qb0D01
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_id2qb0D02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily40

8. Citations (1)

9. Files and Curves (10)