6xlf

Full-length Hsc82 in complex with Aha1 in the presence of AMP-PNP

Method: ELECTRON MICROSCOPY
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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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 4 Hsp90 co-chaperone AHA1 × 2 (Q12449) PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MAGNESIUM ION × 2 POTASSIUM ION × 2 Consistent with protein count

Other States of the Same Protein in the Database

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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 4 ATP-dependent molecular chaperone HSC82 × 2 (P15108) PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MAGNESIUM ION × 2 POTASSIUM ION × 2 Consistent with protein count

Other States of the Same Protein in the Database

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id6xlf
Deposition date deposition_date2020-06-28
Structure title titleFull-length Hsc82 in complex with Aha1 in the presence of AMP-PNP
Keywords keywordsCo-chaperone, activator, CHAPERONE; CHAPERONE
Experimental Method methodELECTRON MICROSCOPY
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

6xlf__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

6xlf__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

6xlf__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)39.15 Å
Rg (electron density)38.28 Å
Total Rg38.81 Å
Atom count13653
Residues1680
Excluded volume244360 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 6xlf__assembly_1__model_1 tetrameric (4) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (5)

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6. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id6xlfC01
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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7. Citations (1)