3fh6

Crystal structure of the resting state maltose transporter from E. coli

Method: X-RAY DIFFRACTION Dmax: 200.3 Å Quality: GOOD

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

Maltose transport system permease protein malF

Escherichia coli

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 F; UniProt 36–514 Not recorded Maltose transport system permease protein malG × 1 (P68183) Maltose/maltodextrin import ATP-binding protein malK × 2 (P68187) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;11.5 % PEG 4000, 0.1M ADA pH 6.5, 0.1 M NaCl, 0.1 M Li2SO4, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 4.50 Å R-free 0.363
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain H; UniProt 36–514 Not recorded Maltose transport system permease protein malG × 1 (P68183) Maltose/maltodextrin import ATP-binding protein malK × 2 (P68187) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;11.5 % PEG 4000, 0.1M ADA pH 6.5, 0.1 M NaCl, 0.1 M Li2SO4, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 4.50 Å R-free 0.363

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 11 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 F; PDBConstruct 2–480; UniProt 36–514 Author chain H; PDBConstruct 2–480; UniProt 36–514

Maltose transport system permease protein malG

Escherichia coli

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 G; UniProt 1–296 Not recorded Maltose transport system permease protein malF × 1 (P02916) Maltose/maltodextrin import ATP-binding protein malK × 2 (P68187) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;11.5 % PEG 4000, 0.1M ADA pH 6.5, 0.1 M NaCl, 0.1 M Li2SO4, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 4.50 Å R-free 0.363
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain I; UniProt 1–296 Not recorded Maltose transport system permease protein malF × 1 (P02916) Maltose/maltodextrin import ATP-binding protein malK × 2 (P68187) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;11.5 % PEG 4000, 0.1M ADA pH 6.5, 0.1 M NaCl, 0.1 M Li2SO4, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 4.50 Å R-free 0.363

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 9 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 G; PDBConstruct 1–296; UniProt 1–296 Author chain I; PDBConstruct 1–296; UniProt 1–296

Maltose/maltodextrin import ATP-binding protein malK

Escherichia coli

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 A; UniProt 1–371 Chain B; UniProt 1–371 Not recorded Maltose transport system permease protein malF × 1 (P02916) Maltose transport system permease protein malG × 1 (P68183) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;11.5 % PEG 4000, 0.1M ADA pH 6.5, 0.1 M NaCl, 0.1 M Li2SO4, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 4.50 Å R-free 0.363
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–371 Chain D; UniProt 1–371 Not recorded Maltose transport system permease protein malF × 1 (P02916) Maltose transport system permease protein malG × 1 (P68183) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;11.5 % PEG 4000, 0.1M ADA pH 6.5, 0.1 M NaCl, 0.1 M Li2SO4, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 4.50 Å R-free 0.363

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 22 assemblies. Open the comparison page and filter oligomeric states

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

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 3fh6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3fh6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3fh6
Deposition date deposition_date2008-12-08
Structure title titleCrystal structure of the resting state maltose transporter from E. coli
Keywords keywords;maltose transporter, ground state, ABC transporter, membrane protein, Cell inner membrane, Cell membrane, Membrane, Sugar transport, Transmembrane, Transport, ATP-binding, Hydrolase, Nucleotide-binding, TRANSPORT PROTEIN ;; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier57.61
Radius of gyration Rg (electron density) rg_electron57.77
Forward intensity I(0) i01046330000.00
Molecular weight molecular_weight287240.0 kDa
Excluded volume excluded_volume366610 ų
Envelope volume envelope_volume567200 ų
Hydration-shell volume shell_volume82930 ų
Envelope diameter envelope_diameter209.5
Shell Rg shell_rg58.11
Envelope Rg envelope_rg56.22
Shape Rg shape_rg57.80
Total Rg total_rg57.66
Total atoms total_atoms20236
Residues n_residues2626
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 dmax200.3
Rg (real space) rg_real57.75
Rg uncertainty (real space) rg_real_error1.90
I(0) (real space) i0_real1.0460e+09
I(0) uncertainty (real space) i0_real_error1.9440e+07
Rg (reciprocal space) rg_reciprocal57.46
I(0) (reciprocal space) i0_reciprocal1046000000.0000
Solution quality estimate total_estimate0.8709
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary51.9
Skewness Skewness skewness0.316
Kurtosis Kurtosis kurtosis-0.494
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha93900000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.858; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.938; Smooth: 0.805

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)