8tlx

Crystal structure of MBP and AF9 AHD fusion protein 3AQA in complex with peptidomimetic inhibitor 21a

Method: X-RAY DIFFRACTION Dmax: 84.5 Å Quality: GOOD

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

MBP and AF9 AHD fusion protein 3AQA

Homo sapiens

UniProt P0AEX9

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 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 27–392 Not recorded peptidomimetic inhibitor 21a × 1 alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;20-30% PEG3350 and 0.1 M Bis-Tris pH 5.5 Resolution 2.10 Å R-free 0.227

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.

366 other PDB entries and 491 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–370; UniProt 27–392

MBP and AF9 AHD fusion protein 3AQA

Homo sapiens

UniProt P42568

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 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 500–568 Not recorded peptidomimetic inhibitor 21a × 1 alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;20-30% PEG3350 and 0.1 M Bis-Tris pH 5.5 Resolution 2.10 Å R-free 0.227

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.

24 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AF9_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 374–442; UniProt 500–568

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 8tlx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8tlx
Deposition date deposition_date2023-07-27
Structure title titleCrystal structure of MBP and AF9 AHD fusion protein 3AQA in complex with peptidomimetic inhibitor 21a
Keywords keywordsMLL fusion Super elongation complex (SEC) acute lymphoblastic leukemia acute myeloid leukemia, TRANSLATION; TRANSLATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.11
Radius of gyration Rg (electron density) rg_electron24.22
Forward intensity I(0) i038424600.00
Molecular weight molecular_weight49214.0 kDa
Excluded volume excluded_volume62068 ų
Envelope volume envelope_volume72886 ų
Hydration-shell volume shell_volume25842 ų
Envelope diameter envelope_diameter88.3
Shell Rg shell_rg30.50
Envelope Rg envelope_rg24.47
Shape Rg shape_rg24.19
Total Rg total_rg25.04
Total atoms total_atoms3475
Residues n_residues444
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 dmax84.5
Rg (real space) rg_real25.12
Rg uncertainty (real space) rg_real_error0.65
I(0) (real space) i0_real3.8420e+07
I(0) uncertainty (real space) i0_real_error5.5620e+05
Rg (reciprocal space) rg_reciprocal25.12
I(0) (reciprocal space) i0_reciprocal38420000.0000
Solution quality estimate total_estimate0.8784
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.8
Skewness Skewness skewness0.368
Kurtosis Kurtosis kurtosis-0.309
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9829000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.845; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.947; Smooth: 0.933

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)