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8eod

EEVD:Sis1-81 (J domain) bound conformation

Method: SOLUTION NMR Dmax: 50.3 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Protein SIS1

Saccharomyces cerevisiae S288C

UniProt P25294

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 2–81 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions：pH 7.2；298 K；Ionic strength (raw mmCIF value) 0.2；Pressure 1 NMR sample composition：500 uM [U-13C; U-15N] 15N-13C-Sis11-81:EEVD, 1 mM [U-90% 15N] 15N-Sis11-81:EEVD, 90% H2O/10% D2O | 90% H2O/10% D2O Resolution not provided

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 8EOD Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1C3G S. CEREVISIAE HEAT SHOCK PROTEIN 40 SIS1 Deposited 1999-07-27 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 180–349（170 aa） Fragment：SIS1 C-TERMINAL PEPTIDE-BINDING DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.2；298 K；PEG 3350 20%, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 25K
Resolution 2.70 Å R-free 0.311
2B26 The crystal structure of the protein complex of yeast Hsp40 Sis1 and Hsp70 Ssa1 Deposited 2005-09-16 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 181–352（172 aa） Fragment：Yeast Hsp40 Sis1 C-terminal domain
Chain B 181–352（172 aa） Fragment：Yeast Hsp40 Sis1 C-terminal domain
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 3.20 Å R-free 0.339
2B26 The crystal structure of the protein complex of yeast Hsp40 Sis1 and Hsp70 Ssa1 Deposited 2005-09-16 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 181–352（172 aa） Fragment：Yeast Hsp40 Sis1 C-terminal domain
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 3.20 Å R-free 0.339
4RWU J-domain of Sis1 protein, Hsp40 co-chaperone from Saccharomyces cerevisiae Deposited 2014-12-05 Different construct Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–89（89 aa） Fragment：J-domain (UNP residues 1-89)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；289 K；2.4 M sodium malonate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K
Resolution 1.25 Å R-free 0.149

3 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SIS1_YEAST
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 5–84； UniProt 2–81

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 8eod

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8eod
Deposition date deposition_date2022-10-03
Structure title titleEEVD:Sis1-81 (J domain) bound conformation
Keywords keywordsJ-domain, Sis1, EEVD, CHAPERONE; CHAPERONE
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier13.26 Å
Radius of gyration Rg (electron density) rg_electron13.11 Å
Forward intensity I(0) i0486628000.00
Molecular weight molecular_weight186970.0 kDa
Excluded volume excluded_volume234040 ų
Envelope volume envelope_volume23796 ų
Hydration-shell volume shell_volume13373 ų
Envelope diameter envelope_diameter52.7 Å
Shell Rg shell_rg21.08 Å
Envelope Rg envelope_rg15.79 Å
Shape Rg shape_rg13.10 Å
Total Rg total_rg13.33 Å
Total atoms total_atoms26240
Residues n_residues1680
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 dmax50.3 Å
Rg (real space) rg_real13.24 Å
Rg uncertainty (real space) rg_real_error0.45 Å
I(0) (real space) i0_real4.8660e+08
I(0) uncertainty (real space) i0_real_error6.0300e+06
Rg (reciprocal space) rg_reciprocal13.24 Å
I(0) (reciprocal space) i0_reciprocal486600000.0000
Solution quality estimate total_estimate0.5682
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary14.6 Å
Skewness Skewness skewness0.233
Kurtosis Kurtosis kurtosis-0.421
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha175800.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.610; Stabil: 1.000; Sysdev: 0.256; Positv: 1.000; Valcen: 0.784; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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9. Files and Curves (10)