5i69

MBP-MamC magnetite-interaction component mutant-D70A

Method: X-RAY DIFFRACTION Dmax: 68.1 Å Quality: EXCELLENT

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

Maltose-binding periplasmic protein,Tightly bound bacterial magnetic particle protein,Maltose-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 Insufficient information Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 27–389 Chain A; UniProt 390–396 Mutation:D70A alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;2M ammonium sulfate and 0.1M sodium citrate pH 4.5 Resolution 2.70 Å R-free 0.293

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 22–384; UniProt 27–389 Author chain A; PDBConstruct 406–412; UniProt 390–396

Maltose-binding periplasmic protein,Tightly bound bacterial magnetic particle protein,Maltose-binding periplasmic protein

Escherichia coli

UniProt Q2W8S0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 57–77 Mutation:D70A alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;2M ammonium sulfate and 0.1M sodium citrate pH 4.5 Resolution 2.70 Å R-free 0.293

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.

2 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q2W8S0_MAGSA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 385–405; UniProt 57–77

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 5i69

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5i69
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5i69
Deposition date deposition_date2016-02-16
Structure title titleMBP-MamC magnetite-interaction component mutant-D70A
Keywords keywordsMagnetotactic bacteria, MamC, Biomineralization, Magnetite, protein-mineral interaction, Magnetite binding protein; Magnetite binding protein
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.97
Radius of gyration Rg (electron density) rg_electron20.84
Forward intensity I(0) i028321300.00
Molecular weight molecular_weight42149.0 kDa
Excluded volume excluded_volume53299 ų
Envelope volume envelope_volume62157 ų
Hydration-shell volume shell_volume24408 ų
Envelope diameter envelope_diameter70.9
Shell Rg shell_rg27.89
Envelope Rg envelope_rg21.09
Shape Rg shape_rg20.79
Total Rg total_rg21.88
Total atoms total_atoms2977
Residues n_residues380
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 dmax68.1
Rg (real space) rg_real21.85
Rg uncertainty (real space) rg_real_error0.27
I(0) (real space) i0_real2.8320e+07
I(0) uncertainty (real space) i0_real_error3.2070e+05
Rg (reciprocal space) rg_reciprocal21.88
I(0) (reciprocal space) i0_reciprocal28320000.0000
Solution quality estimate total_estimate0.9023
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.4
Skewness Skewness skewness0.206
Kurtosis Kurtosis kurtosis-0.438
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6860000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.917; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.977

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd5i69a_
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

8. Citations (1)

9. Files and Curves (10)