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6xlc

Full-length Hsc82 bound to AMPPNP

Method: ELECTRON MICROSCOPY Dmax: 130.1 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

ATP-dependent molecular chaperone HSC82

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P15108

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 1–705 Chain B； UniProt 1–705 Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.66 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.

Other PDB Difference from Current Entry 6XLC Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
6XLB Apo full-length Hsc82 in complex with Aha1 Deposited 2020-06-28 Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–705（705 aa）
Chain B 1–705（705 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.80 Å
6XLD Full-length Hsc82 in complex with Aha1 CTD in the presence of AMPPNP Deposited 2020-06-28 Different oligomeric state Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 1–705（705 aa）
Chain B 1–705（705 aa）
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.66 Å
6XLE Full-length Hsc82 in complex with two Aha1 CTD in the presence of AMP-PNP Deposited 2020-06-28 Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–705（705 aa）
Chain B 1–705（705 aa）
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 K POTASSIUM ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.74 Å
6XLF Full-length Hsc82 in complex with Aha1 in the presence of AMP-PNP Deposited 2020-06-28 Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–705（705 aa）
Chain B 1–705（705 aa）
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 K POTASSIUM ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.15 Å
6XLG Full-length Hsc82 in complex with two Aha1 CTD in the presence of ATPgammaS Deposited 2020-06-28 Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–705（705 aa）
Chain B 1–705（705 aa）
Not recorded AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 K POTASSIUM ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.71 Å
6XLH Asymmetric hydrolysis state of Hsc82 in complex with Aha1 bound with ADP and ATPgammaS Deposited 2020-06-28 Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–705（705 aa）
Chain B 1–705（705 aa）
Not recorded AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 2 K POTASSIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.83 Å

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HSC82_YEAST
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–705； UniProt 1–705 Author chain B； PDBConstruct 1–705； UniProt 1–705

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 6xlc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6xlc
Deposition date deposition_date2020-06-28
Structure title titleFull-length Hsc82 bound to AMPPNP
Keywords keywordsHsp90, CHAPERONE; CHAPERONE
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier39.22 Å
Radius of gyration Rg (electron density) rg_electron38.66 Å
Forward intensity I(0) i0280031000.00
Molecular weight molecular_weight139830.0 kDa
Excluded volume excluded_volume176650 ų
Envelope volume envelope_volume234280 ų
Hydration-shell volume shell_volume50671 ų
Envelope diameter envelope_diameter127.4 Å
Shell Rg shell_rg44.30 Å
Envelope Rg envelope_rg38.11 Å
Shape Rg shape_rg38.64 Å
Total Rg total_rg39.06 Å
Total atoms total_atoms9858
Residues n_residues1212
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax130.1 Å
Rg (real space) rg_real39.25 Å
Rg uncertainty (real space) rg_real_error1.06 Å
I(0) (real space) i0_real2.8000e+08
I(0) uncertainty (real space) i0_real_error4.7800e+06
Rg (reciprocal space) rg_reciprocal39.23 Å
I(0) (reciprocal space) i0_reciprocal280000000.0000
Solution quality estimate total_estimate0.8954
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary45.5 Å
Skewness Skewness skewness0.289
Kurtosis Kurtosis kurtosis-0.552
Angular range angular_range— – 0.2000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha65860000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.909; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.940
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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8. Citations (1)

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9. Files and Curves (10)