9bcr

Cryo-EM structure of a bacterial prototype ATP-binding cassette transporter MalFGK2.

Method: ELECTRON MICROSCOPY Dmax: 135.9 Å Quality: GOOD

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

Maltose/maltodextrin transport system permease protein MalF

Escherichia coli K-12

UniProt P02916

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain H; UniProt 1–514 Not recorded Maltose/maltodextrin transport system permease protein MalG × 1 (P68183) Maltose/maltodextrin import ATP-binding protein MalK × 1 (P68187) Maltose/maltodextrin import ATP-binding protein MalK × 1 (P68187) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.26 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.

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

View Construct and Data Evidence
UniProt name MALF_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain H; PDBConstruct 1–514; UniProt 1–514

Maltose/maltodextrin transport system permease protein MalG

Escherichia coli K-12

UniProt P68183

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain I; UniProt 2–287 Not recorded Maltose/maltodextrin transport system permease protein MalF × 1 (P02916) Maltose/maltodextrin import ATP-binding protein MalK × 1 (P68187) Maltose/maltodextrin import ATP-binding protein MalK × 1 (P68187) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.26 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.

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

View Construct and Data Evidence
UniProt name MALG_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain I; PDBConstruct 1–286; UniProt 2–287

Maltose/maltodextrin import ATP-binding protein MalK

Escherichia coli K-12

UniProt P68187

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 2–371 Chain D; UniProt 2–371 Not recorded Maltose/maltodextrin transport system permease protein MalF × 1 (P02916) Maltose/maltodextrin transport system permease protein MalG × 1 (P68183) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.26 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.

13 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALK_ECOLI
Isoform
PDB entities 3, 4
Chains and sequence ranges Author chain C; PDBConstruct 1–370; UniProt 2–371 Author chain D; PDBConstruct 1–370; UniProt 2–371

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 9bcr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9bcr
Deposition date deposition_date2024-04-09
Structure title titleCryo-EM structure of a bacterial prototype ATP-binding cassette transporter MalFGK2.
Keywords keywordsbacterial prototype ATP-binding cassette transporter, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.97
Radius of gyration Rg (electron density) rg_electron40.38
Forward intensity I(0) i0303174000.00
Molecular weight molecular_weight150230.0 kDa
Excluded volume excluded_volume191640 ų
Envelope volume envelope_volume264690 ų
Hydration-shell volume shell_volume55247 ų
Envelope diameter envelope_diameter144.5
Shell Rg shell_rg45.65
Envelope Rg envelope_rg39.42
Shape Rg shape_rg40.42
Total Rg total_rg40.52
Total atoms total_atoms10595
Residues n_residues1368
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 dmax135.9
Rg (real space) rg_real41.02
Rg uncertainty (real space) rg_real_error1.38
I(0) (real space) i0_real3.0320e+08
I(0) uncertainty (real space) i0_real_error5.9180e+06
Rg (reciprocal space) rg_reciprocal40.97
I(0) (reciprocal space) i0_reciprocal303200000.0000
Solution quality estimate total_estimate0.8847
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary48.8
Skewness Skewness skewness0.354
Kurtosis Kurtosis kurtosis-0.433
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha38200000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.890; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.969; Smooth: 0.859

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)