9fkq

Cryo-EM structure of MBP homo-dimer assembled by homo Di-Gluebody - MBP local refinement

Method: ELECTRON MICROSCOPY Dmax: 70.9 Å Quality: EXCELLENT

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

Maltose/maltodextrin-binding periplasmic protein

Escherichia coli

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 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 27–392 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.45 Å

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 2–367; UniProt 27–392

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 9fkq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9fkq
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9fkq
Deposition date deposition_date2024-06-03
Structure title titleCryo-EM structure of MBP homo-dimer assembled by homo Di-Gluebody - MBP local refinement
Keywords keywordsGluebody, Nanobody, cryo-EM SPA, small protein, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier22.52
Radius of gyration Rg (electron density) rg_electron21.47
Forward intensity I(0) i025081600.00
Molecular weight molecular_weight39683.0 kDa
Excluded volume excluded_volume50233 ų
Envelope volume envelope_volume58266 ų
Hydration-shell volume shell_volume22656 ų
Envelope diameter envelope_diameter71.6
Shell Rg shell_rg27.95
Envelope Rg envelope_rg21.53
Shape Rg shape_rg21.41
Total Rg total_rg22.48
Total atoms total_atoms5577
Residues n_residues362
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 dmax70.9
Rg (real space) rg_real22.47
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real2.5080e+07
I(0) uncertainty (real space) i0_real_error3.3210e+05
Rg (reciprocal space) rg_reciprocal22.48
I(0) (reciprocal space) i0_reciprocal25080000.0000
Solution quality estimate total_estimate0.9055
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.8
Skewness Skewness skewness0.270
Kurtosis Kurtosis kurtosis-0.415
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4843000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.925; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)