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6xlh

Asymmetric hydrolysis state of Hsc82 in complex with Aha1 bound with ADP and ATPgammaS

Method: ELECTRON MICROSCOPY Dmax: 125.2 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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain A； UniProt 1–705 Chain B； UniProt 1–705 Not recorded Hsp90 co-chaperone AHA1 × 2 （Q12449） 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

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 6XLH 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 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
6XLC Full-length Hsc82 bound to AMPPNP Deposited 2020-06-28 Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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
6XLD Full-length Hsc82 in complex with Aha1 CTD in the presence of AMPPNP Deposited 2020-06-28 Different oligomeric state Different ligand/ion Different structure-quality metrics 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 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 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 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

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

Hsp90 co-chaperone AHA1

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt Q12449

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 × 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain C； UniProt 1–350 Chain D； UniProt 1–350 Not recorded ATP-dependent molecular chaperone HSC82 × 2 （P15108） 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

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 6XLH Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1USU The Structure of the complex between Aha1 and HSP90 Deposited 2003-12-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–156（156 aa） Fragment：N-TERMINAL DOMAIN, RESIDUES 1-156
Not recorded GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；pH 6.5；292 K；CRYSTALS GREW FROM A MIXTURE OF MIDDLE DOMAIN HSP90 AND N- TERMINAL AHA1 AT A FINAL CONCENTRATION OF 110 UM AND 165 UM, RESPECTIVELY, IN A SOLUTION CONTAINING 90 MM AMMONIUM SULPHATE, 13.5% (W/V) PEG8K AND 45 MM SODIUM CACODYLATE PH 6.5 IN UNDER-OIL MICROBATCH EXPERIMENTS AT 19C.
Resolution 2.15 Å R-free 0.268
1USV The Structure of the complex between Aha1 and HSP90 Deposited 2003-12-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–156（156 aa） Fragment：N-TERMINAL DOMAIN, RESIDUES 1-156
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；pH 6.5；292 K；CRYSTALS GREW FROM A MIXTURE OF MIDDLE DOMAIN HSP90 AND N- TERMINAL AHA1 AT A FINAL CONCENTRATION OF 110 UM AND 165 UM, RESPECTIVELY, IN A SOLUTION CONTAINING 90 MM AMMONIUM SULPHATE, 13.5% (W/V) PEG8K AND 45 MM SODIUM CACODYLATE PH 6.5 IN UNDER-OIL MICROBATCH EXPERIMENTS AT 19C.
Resolution 2.70 Å R-free 0.298
1USV The Structure of the complex between Aha1 and HSP90 Deposited 2003-12-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 1–156（156 aa） Fragment：N-TERMINAL DOMAIN, RESIDUES 1-156
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；pH 6.5；292 K；CRYSTALS GREW FROM A MIXTURE OF MIDDLE DOMAIN HSP90 AND N- TERMINAL AHA1 AT A FINAL CONCENTRATION OF 110 UM AND 165 UM, RESPECTIVELY, IN A SOLUTION CONTAINING 90 MM AMMONIUM SULPHATE, 13.5% (W/V) PEG8K AND 45 MM SODIUM CACODYLATE PH 6.5 IN UNDER-OIL MICROBATCH EXPERIMENTS AT 19C.
Resolution 2.70 Å R-free 0.298
1USV The Structure of the complex between Aha1 and HSP90 Deposited 2003-12-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain F 1–156（156 aa） Fragment：N-TERMINAL DOMAIN, RESIDUES 1-156
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；pH 6.5；292 K；CRYSTALS GREW FROM A MIXTURE OF MIDDLE DOMAIN HSP90 AND N- TERMINAL AHA1 AT A FINAL CONCENTRATION OF 110 UM AND 165 UM, RESPECTIVELY, IN A SOLUTION CONTAINING 90 MM AMMONIUM SULPHATE, 13.5% (W/V) PEG8K AND 45 MM SODIUM CACODYLATE PH 6.5 IN UNDER-OIL MICROBATCH EXPERIMENTS AT 19C.
Resolution 2.70 Å R-free 0.298
1USV The Structure of the complex between Aha1 and HSP90 Deposited 2003-12-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain H 1–156（156 aa） Fragment：N-TERMINAL DOMAIN, RESIDUES 1-156
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；pH 6.5；292 K；CRYSTALS GREW FROM A MIXTURE OF MIDDLE DOMAIN HSP90 AND N- TERMINAL AHA1 AT A FINAL CONCENTRATION OF 110 UM AND 165 UM, RESPECTIVELY, IN A SOLUTION CONTAINING 90 MM AMMONIUM SULPHATE, 13.5% (W/V) PEG8K AND 45 MM SODIUM CACODYLATE PH 6.5 IN UNDER-OIL MICROBATCH EXPERIMENTS AT 19C.
Resolution 2.70 Å R-free 0.298
6XLB Apo full-length Hsc82 in complex with Aha1 Deposited 2020-06-28 Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C1 1–350（350 aa）
Chain D1 1–350（350 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 construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain C 1–350（350 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 ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 1–350（350 aa）
Chain D 1–350（350 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 ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 1–350（350 aa）
Chain D 1–350（350 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 ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 1–350（350 aa）
Chain D 1–350（350 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

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

View Construct and Data Evidence
UniProt name AHA1_YEAST
Isoform —
PDB entities 2
Chains and sequence ranges Author chain C； PDBConstruct 1–350； UniProt 1–350 Author chain D； PDBConstruct 1–350； UniProt 1–350

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 6xlh

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6xlh
Deposition date deposition_date2020-06-28
Structure title titleAsymmetric hydrolysis state of Hsc82 in complex with Aha1 bound with ADP and ATPgammaS
Keywords keywordsCo-chaperone, activator, 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_guinier39.15 Å
Radius of gyration Rg (electron density) rg_electron38.26 Å
Forward intensity I(0) i0527951000.00
Molecular weight molecular_weight192850.0 kDa
Excluded volume excluded_volume243640 ų
Envelope volume envelope_volume322220 ų
Hydration-shell volume shell_volume68225 ų
Envelope diameter envelope_diameter127.7 Å
Shell Rg shell_rg45.74 Å
Envelope Rg envelope_rg37.77 Å
Shape Rg shape_rg38.23 Å
Total Rg total_rg38.80 Å
Total atoms total_atoms13608
Residues n_residues1675
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 dmax125.2 Å
Rg (real space) rg_real38.95 Å
Rg uncertainty (real space) rg_real_error0.87 Å
I(0) (real space) i0_real5.2800e+08
I(0) uncertainty (real space) i0_real_error8.1060e+06
Rg (reciprocal space) rg_reciprocal39.08 Å
I(0) (reciprocal space) i0_reciprocal528000000.0000
Solution quality estimate total_estimate0.8884
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary50.1 Å
Skewness Skewness skewness0.217
Kurtosis Kurtosis kurtosis-0.391
Angular range angular_range— – 0.2000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha77770000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.888; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.891
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id6xlhC01
Class class3 — Alpha Beta
Architecture architecture15 — Super Roll
Topology topology10 — Bactericidal permeability-increasing protein; domain 1
Homologous superfamily homologous superfamily20 — Activator of Hsp90 ATPase Aha1, N-terminal domain
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8. Citations (1)

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9. Files and Curves (10)