8eoa

Cryo-EM structure of human HSP90B-AIPL1 complex

Method: ELECTRON MICROSCOPY Dmax: 128.5 Å Quality: GOOD

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

Heat shock protein HSP 90-beta

Homo sapiens

UniProt P08238

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 2–724 Chain B; UniProt 2–724 Not recorded Aryl-hydrocarbon-interacting protein-like 1 × 1 (Q924K1) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;25 mM HEPES, 200 mM NaCl, 1 mM TCEP, pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

29 other PDB entries and 50 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HS90B_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 34–756; UniProt 2–724 Author chain B; PDBConstruct 34–756; UniProt 2–724

Aryl-hydrocarbon-interacting protein-like 1

Mus musculus

UniProt Q924K1

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–328 Not recorded Heat shock protein HSP 90-beta × 2 (P08238) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;25 mM HEPES, 200 mM NaCl, 1 mM TCEP, pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name AIPL1_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 23–350; UniProt 1–328

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 8eoa

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8eoa
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8eoa
Deposition date deposition_date2022-10-02
Structure title titleCryo-EM structure of human HSP90B-AIPL1 complex
Keywords keywordsHSP90B, AIPL1, phosphodiesterase 6, CHAPERONE; CHAPERONE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.42
Radius of gyration Rg (electron density) rg_electron38.72
Forward intensity I(0) i0402748000.00
Molecular weight molecular_weight164250.0 kDa
Excluded volume excluded_volume206070 ų
Envelope volume envelope_volume281460 ų
Hydration-shell volume shell_volume60087 ų
Envelope diameter envelope_diameter131.2
Shell Rg shell_rg44.97
Envelope Rg envelope_rg38.31
Shape Rg shape_rg38.72
Total Rg total_rg39.09
Total atoms total_atoms11535
Residues n_residues1421
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 dmax128.5
Rg (real space) rg_real39.31
Rg uncertainty (real space) rg_real_error0.90
I(0) (real space) i0_real4.0270e+08
I(0) uncertainty (real space) i0_real_error6.9200e+06
Rg (reciprocal space) rg_reciprocal39.38
I(0) (reciprocal space) i0_reciprocal402800000.0000
Solution quality estimate total_estimate0.8978
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.2
Skewness Skewness skewness0.238
Kurtosis Kurtosis kurtosis-0.481
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha102700000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.908; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.945

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)