1jvy

Maltodextrin-binding protein variant D207C/A301GS/P316C with beta-mercaptoethanol mixed disulfides

Method: X-RAY DIFFRACTION Dmax: 68.5 Å Quality: GOOD

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 Mutation:D207C/A301GS/P316C Non-standard monomer:Yes (specific site not provided by mmCIF) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.2;277 K;PEG 6000, sodium MES, maltose, sodium azide, beta-mercaptoethanol, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.90 Å R-free 0.273

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 2–372; 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 1jvy

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1jvy
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1jvy
Deposition date deposition_date2001-08-31
Structure title titleMaltodextrin-binding protein variant D207C/A301GS/P316C with beta-mercaptoethanol mixed disulfides
Keywords keywordsintermolecular, cross-link, disulfide, 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_guinier21.74
Radius of gyration Rg (electron density) rg_electron20.63
Forward intensity I(0) i027200000.00
Molecular weight molecular_weight41265.0 kDa
Excluded volume excluded_volume52158 ų
Envelope volume envelope_volume58736 ų
Hydration-shell volume shell_volume23472 ų
Envelope diameter envelope_diameter71.7
Shell Rg shell_rg27.54
Envelope Rg envelope_rg20.83
Shape Rg shape_rg20.58
Total Rg total_rg21.66
Total atoms total_atoms2911
Residues n_residues369
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 dmax68.5
Rg (real space) rg_real21.63
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real2.7200e+07
I(0) uncertainty (real space) i0_real_error3.4660e+05
Rg (reciprocal space) rg_reciprocal21.65
I(0) (reciprocal space) i0_reciprocal27200000.0000
Solution quality estimate total_estimate0.8997
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.6
Skewness Skewness skewness0.218
Kurtosis Kurtosis kurtosis-0.422
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5989000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.902; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.986

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_idd1jvya_
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_id1jvyA01
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_id1jvyA02
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 (1)

9. Files and Curves (10)