9bdt

Apolipoprotein B 100 bound to LDL receptor and legobody

Method: ELECTRON MICROSCOPY Dmax: 342.6 Å Quality: GOOD

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

Apolipoprotein B-100

OrganismNot specified

UniProt P04114

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 Heteromer Protein × 7 其他Polymer 1 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 1–4563 Not recorded Legobody 8D3 Fab Heavy Chain × 1 Legobody 8D3 Fab Light Chain × 1 Maltodextrin-binding protein,Immunoglobulin G-binding protein A,Immunoglobulin G-binding protein G × 1 (C3SHQ8,P99134,P06654) Low-density lipoprotein receptor × 2 (P01130) ApoB100 nanobody 4 × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 CA CALCIUM ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.40 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name APOB_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–4563; UniProt 1–4563

Maltodextrin-binding protein,Immunoglobulin G-binding protein A,Immunoglobulin G-binding protein G

Escherichia coli

UniProt C3SHQ8

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 Heteromer Protein × 7 其他Polymer 1 PDB declaration: heptameric(7) Consistent with protein copy count Chain B; UniProt 27–384 Not recorded Apolipoprotein B-100 × 1 (P04114) Legobody 8D3 Fab Heavy Chain × 1 Legobody 8D3 Fab Light Chain × 1 Low-density lipoprotein receptor × 2 (P01130) ApoB100 nanobody 4 × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 CA CALCIUM ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.40 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.

15 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C3SHQ8_ECOLX
Isoform
PDB entities 4
Chains and sequence ranges Author chain B; PDBConstruct 2–359; UniProt 27–384

Maltodextrin-binding protein,Immunoglobulin G-binding protein A,Immunoglobulin G-binding protein G

Escherichia coli

UniProt P06654

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 Heteromer Protein × 7 其他Polymer 1 PDB declaration: heptameric(7) Consistent with protein copy count Chain B; UniProt 295–352 Not recorded Apolipoprotein B-100 × 1 (P04114) Legobody 8D3 Fab Heavy Chain × 1 Legobody 8D3 Fab Light Chain × 1 Low-density lipoprotein receptor × 2 (P01130) ApoB100 nanobody 4 × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 CA CALCIUM ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.40 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.

48 other PDB entries and 54 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPG1_STRSG
Isoform
PDB entities 4
Chains and sequence ranges Author chain B; PDBConstruct 479–536; UniProt 295–352

Maltodextrin-binding protein,Immunoglobulin G-binding protein A,Immunoglobulin G-binding protein G

Escherichia coli

UniProt P99134

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 Heteromer Protein × 7 其他Polymer 1 PDB declaration: heptameric(7) Consistent with protein copy count Chain B; UniProt 43–151 Not recorded Apolipoprotein B-100 × 1 (P04114) Legobody 8D3 Fab Heavy Chain × 1 Legobody 8D3 Fab Light Chain × 1 Low-density lipoprotein receptor × 2 (P01130) ApoB100 nanobody 4 × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 CA CALCIUM ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.40 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPA_STAAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain B; PDBConstruct 360–467; UniProt 43–151

Low-density lipoprotein receptor

Homo sapiens

UniProt P01130

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 Heteromer Protein × 7 其他Polymer 1 PDB declaration: heptameric(7) Consistent with protein copy count Chain I; UniProt 1–860 Chain R; UniProt 1–860 Not recorded Apolipoprotein B-100 × 1 (P04114) Legobody 8D3 Fab Heavy Chain × 1 Legobody 8D3 Fab Light Chain × 1 Maltodextrin-binding protein,Immunoglobulin G-binding protein A,Immunoglobulin G-binding protein G × 1 (C3SHQ8,P99134,P06654) ApoB100 nanobody 4 × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 CA CALCIUM ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.40 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.

33 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LDLR_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain I; PDBConstruct 1–860; UniProt 1–860 Author chain R; PDBConstruct 1–860; UniProt 1–860

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 9bdt

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9bdt
Deposition date deposition_date2024-04-12
Structure title titleApolipoprotein B 100 bound to LDL receptor and legobody
Keywords keywordsLDL, ApoB100, LDL receptor, LIPID TRANSPORT; LIPID TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron114.30
Forward intensity I(0) i04200570000.00
Molecular weight molecular_weight552380.0 kDa
Excluded volume excluded_volume690960 ų
Envelope volume envelope_volume2387300 ų
Hydration-shell volume shell_volume193660 ų
Envelope diameter envelope_diameter341.3
Shell Rg shell_rg106.40
Envelope Rg envelope_rg95.24
Shape Rg shape_rg114.30
Total Rg total_rg114.20
Total atoms total_atoms38899
Residues n_residues5048
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 dmax342.6
Rg (real space) rg_real116.90
Rg uncertainty (real space) rg_real_error1.71
I(0) (real space) i0_real4.1760e+09
I(0) uncertainty (real space) i0_real_error9.6840e+07
Rg (reciprocal space) rg_reciprocal111.10
I(0) (reciprocal space) i0_reciprocal4138000000.0000
Solution quality estimate total_estimate0.8675
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary171.3
Skewness Skewness skewness0.039
Kurtosis Kurtosis kurtosis-0.869
Angular range angular_range— – 0.0700 −1
Current regularization parameter α current_alpha1.3420
Highest regularization parameter α highest_alpha162800000.0000
Real-space data points n_real_points15
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.957; Stabil: 0.883; Sysdev: 1.000; Positv: 1.000; Valcen: 0.766; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)