6bf9

Cryo-EM structure of human insulin degrading enzyme in complex with FAB H11-E heavy chain, FAB H11-E light chain

Method: ELECTRON MICROSCOPY Dmax: 157.8 Å Quality: GOOD

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

Insulin-degrading enzyme

Homo sapiens

UniProt P14735

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 46–1011 Chain B; UniProt 46–1011 Fragment:residues 46-1011 Fab H11-E heavy chain × 2 (P0DOX5) Fab H11-E light chain × 2 (P0DOX7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE;The cryo grids were made using Spotiton Resolution 7.20 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.

55 other PDB entries and 96 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IDE_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–966; UniProt 46–1011 Author chain B; PDBConstruct 1–966; UniProt 46–1011

Fab H11-E heavy chain

Homo sapiens

UniProt P0DOX5

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 125–219 Chain E; UniProt 125–219 Not recorded Insulin-degrading enzyme × 2 (P14735) Fab H11-E light chain × 2 (P0DOX7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE;The cryo grids were made using Spotiton Resolution 7.20 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.

105 other PDB entries and 128 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGG1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 124–218; UniProt 125–219 Author chain E; PDBConstruct 124–218; UniProt 125–219

Fab H11-E light chain

Homo sapiens

UniProt P0DOX7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain D; UniProt 109–211 Chain F; UniProt 109–211 Not recorded Insulin-degrading enzyme × 2 (P14735) Fab H11-E heavy chain × 2 (P0DOX5) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE;The cryo grids were made using Spotiton Resolution 7.20 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.

18 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGK_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 109–211; UniProt 109–211 Author chain F; PDBConstruct 109–211; UniProt 109–211

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 6bf9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6bf9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6bf9
Deposition date deposition_date2017-10-26
Structure title titleCryo-EM structure of human insulin degrading enzyme in complex with FAB H11-E heavy chain, FAB H11-E light chain
Keywords keywordsIDE, amyloid beta, HYDROLASE-IMMUNE SYSTEM complex; HYDROLASE/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier56.90
Radius of gyration Rg (electron density) rg_electron56.40
Forward intensity I(0) i01312980000.00
Molecular weight molecular_weight309070.0 kDa
Excluded volume excluded_volume388910 ų
Envelope volume envelope_volume616830 ų
Hydration-shell volume shell_volume91992 ų
Envelope diameter envelope_diameter168.7
Shell Rg shell_rg58.87
Envelope Rg envelope_rg53.85
Shape Rg shape_rg56.39
Total Rg total_rg56.51
Total atoms total_atoms21836
Residues n_residues2743
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 dmax157.8
Rg (real space) rg_real56.70
Rg uncertainty (real space) rg_real_error1.31
I(0) (real space) i0_real1.3130e+09
I(0) uncertainty (real space) i0_real_error2.7100e+07
Rg (reciprocal space) rg_reciprocal57.04
I(0) (reciprocal space) i0_reciprocal1314000000.0000
Solution quality estimate total_estimate0.8464
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary90.2
Skewness Skewness skewness0.027
Kurtosis Kurtosis kurtosis-0.823
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha87500000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 1.000; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)