4mbp

MALTODEXTRIN BINDING PROTEIN WITH BOUND MALTETROSE

Method: X-RAY DIFFRACTION Dmax: 67.4 Å Quality: EXCELLENT

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

MALTODEXTRIN BINDING PROTEIN

Escherichia coli

UniProt P02928

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 27–396 Not recorded alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.2;PROTEIN WAS CRYSTALLIZED FROM 18% PEG 8000, 10 MM CITRATE, PH 6.2 Resolution 1.70 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.

41 other PDB entries and 51 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 1–370; UniProt 27–396

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 4mbp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4mbp
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4mbp
Deposition date deposition_date1997-08-17
Structure title titleMALTODEXTRIN BINDING PROTEIN WITH BOUND MALTETROSE
Keywords keywordsPERIPLASMIC BINDING PROTEIN, TRANSPORT, SUGAR TRANSPORT; PERIPLASMIC BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.86
Radius of gyration Rg (electron density) rg_electron20.76
Forward intensity I(0) i027027700.00
Molecular weight molecular_weight41277.0 kDa
Excluded volume excluded_volume52229 ų
Envelope volume envelope_volume59346 ų
Hydration-shell volume shell_volume23612 ų
Envelope diameter envelope_diameter68.1
Shell Rg shell_rg27.48
Envelope Rg envelope_rg20.91
Shape Rg shape_rg20.72
Total Rg total_rg21.75
Total atoms total_atoms2917
Residues n_residues370
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 dmax67.4
Rg (real space) rg_real21.74
Rg uncertainty (real space) rg_real_error0.35
I(0) (real space) i0_real2.7030e+07
I(0) uncertainty (real space) i0_real_error3.4460e+05
Rg (reciprocal space) rg_reciprocal21.77
I(0) (reciprocal space) i0_reciprocal27030000.0000
Solution quality estimate total_estimate0.9059
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.1
Skewness Skewness skewness0.218
Kurtosis Kurtosis kurtosis-0.428
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5579000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.926; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4mbpa_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.94 — Periplasmic binding protein-like II
Superfamily Superfamily superfamilyc.94.1 — Periplasmic binding protein-like II
Family Family familyc.94.1.1 — Phosphate binding protein-like

CATH v4.4 (2 domains)

Domain ID domain_id4mbpA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id4mbpA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II

8. Citations (4)

9. Files and Curves (10)