9xko

High-resolution cryo-EM structure of Maltose Binding Protein

Method: ELECTRON MICROSCOPY Dmax: 67.7 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 Other combination Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 27–392 Not recorded alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.35 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 9xko

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9xko
Deposition date deposition_date2025-11-06
Structure title titleHigh-resolution cryo-EM structure of Maltose Binding Protein
Keywords keywordssmall protein-ligand complex, SUGAR BINDING PROTEIN; SUGAR BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier21.70
Radius of gyration Rg (electron density) rg_electron20.55
Forward intensity I(0) i026355200.00
Molecular weight molecular_weight40679.0 kDa
Excluded volume excluded_volume51443 ų
Envelope volume envelope_volume57813 ų
Hydration-shell volume shell_volume23225 ų
Envelope diameter envelope_diameter70.9
Shell Rg shell_rg27.46
Envelope Rg envelope_rg20.74
Shape Rg shape_rg20.51
Total Rg total_rg21.58
Total atoms total_atoms2876
Residues n_residues368
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 dmax67.7
Rg (real space) rg_real21.59
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real2.6360e+07
I(0) uncertainty (real space) i0_real_error3.3640e+05
Rg (reciprocal space) rg_reciprocal21.61
I(0) (reciprocal space) i0_reciprocal26360000.0000
Solution quality estimate total_estimate0.9026
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.3
Skewness Skewness skewness0.225
Kurtosis Kurtosis kurtosis-0.413
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5617000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.914; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)