9bde

Middle Region of Apolipoprotein B 100 bound to Low Density Lipoprotein Receptor

Method: ELECTRON MICROSCOPY Dmax: 211.7 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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–4563 Not recorded Legobody 8D3 Fab Heavy Chain × 1 Legobody 8D3 Fab light chain × 1 Maltose/maltodextrin-binding periplasmic protein,Immunoglobulin G-binding protein A,Immunoglobulin G-binding protein G × 1 (P0AEX9,P02976,P19909) ApoB100 nanobody 4 × 1 Low-density lipoprotein receptor × 1 (P01130) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 CA CALCIUM ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.18 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 2
Chains and sequence ranges Author chain A; PDBConstruct 1–4563; UniProt 1–4563

Maltose/maltodextrin-binding periplasmic protein,Immunoglobulin G-binding protein A,Immunoglobulin G-binding protein G

;Streptococcus sp. 'group G' ;

UniProt P02976

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 278–327 Chain B; UniProt 103–151 Fragment:;residues 27-384 (Uniprot numbering),residues 278-327 (Uniprot numbering),103-151 (Uniprot numbering),residues 440-497 (Uniprot numbering) ; Legobody 8D3 Fab Heavy Chain × 1 Apolipoprotein B 100 × 1 (P04114) Legobody 8D3 Fab light chain × 1 ApoB100 nanobody 4 × 1 Low-density lipoprotein receptor × 1 (P01130) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 CA CALCIUM ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.18 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.

10 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPA_STAA8
Isoform
PDB entities 4
Chains and sequence ranges Author chain B; PDBConstruct 360–409; UniProt 278–327 Author chain B; PDBConstruct 419–467; UniProt 103–151

Maltose/maltodextrin-binding periplasmic protein,Immunoglobulin G-binding protein A,Immunoglobulin G-binding protein G

;Streptococcus sp. 'group G' ;

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 Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 27–384 Fragment:;residues 27-384 (Uniprot numbering),residues 278-327 (Uniprot numbering),103-151 (Uniprot numbering),residues 440-497 (Uniprot numbering) ; Legobody 8D3 Fab Heavy Chain × 1 Apolipoprotein B 100 × 1 (P04114) Legobody 8D3 Fab light chain × 1 ApoB100 nanobody 4 × 1 Low-density lipoprotein receptor × 1 (P01130) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 CA CALCIUM ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.18 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.

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 4
Chains and sequence ranges Author chain B; PDBConstruct 2–359; UniProt 27–384

Maltose/maltodextrin-binding periplasmic protein,Immunoglobulin G-binding protein A,Immunoglobulin G-binding protein G

;Streptococcus sp. 'group G' ;

UniProt P19909

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 440–497 Fragment:;residues 27-384 (Uniprot numbering),residues 278-327 (Uniprot numbering),103-151 (Uniprot numbering),residues 440-497 (Uniprot numbering) ; Legobody 8D3 Fab Heavy Chain × 1 Apolipoprotein B 100 × 1 (P04114) Legobody 8D3 Fab light chain × 1 ApoB100 nanobody 4 × 1 Low-density lipoprotein receptor × 1 (P01130) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 CA CALCIUM ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.18 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.

76 other PDB entries and 116 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPG2_STRSG
Isoform
PDB entities 4
Chains and sequence ranges Author chain B; PDBConstruct 479–536; UniProt 440–497

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain R; UniProt 1–860 Not recorded Legobody 8D3 Fab Heavy Chain × 1 Apolipoprotein B 100 × 1 (P04114) Legobody 8D3 Fab light chain × 1 Maltose/maltodextrin-binding periplasmic protein,Immunoglobulin G-binding protein A,Immunoglobulin G-binding protein G × 1 (P0AEX9,P02976,P19909) ApoB100 nanobody 4 × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 CA CALCIUM ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.18 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 6
Chains and sequence ranges 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 9bde

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9bde
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9bde
Deposition date deposition_date2024-04-11
Structure title titleMiddle Region of Apolipoprotein B 100 bound to Low Density Lipoprotein Receptor
Keywords keywordsApolipoprotein B 100, ApoB100, LDLreceptor, LIPID TRANSPORT; LIPID TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier71.84
Radius of gyration Rg (electron density) rg_electron72.28
Forward intensity I(0) i0905575000.00
Molecular weight molecular_weight244510.0 kDa
Excluded volume excluded_volume302280 ų
Envelope volume envelope_volume639750 ų
Hydration-shell volume shell_volume80382 ų
Envelope diameter envelope_diameter235.6
Shell Rg shell_rg62.33
Envelope Rg envelope_rg71.43
Shape Rg shape_rg72.24
Total Rg total_rg72.19
Total atoms total_atoms17216
Residues n_residues2340
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 dmax211.7
Rg (real space) rg_real72.12
Rg uncertainty (real space) rg_real_error1.99
I(0) (real space) i0_real9.0500e+08
I(0) uncertainty (real space) i0_real_error2.0760e+07
Rg (reciprocal space) rg_reciprocal70.20
I(0) (reciprocal space) i0_reciprocal901900000.0000
Solution quality estimate total_estimate0.8185
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary57.7
Skewness Skewness skewness0.340
Kurtosis Kurtosis kurtosis-0.848
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0023
Highest regularization parameter α highest_alpha47110000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.936; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.828; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)