SAXSdb — 1c3g

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

HEAT SHOCK PROTEIN 40

Saccharomyces cerevisiae

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 180–349	Fragment：SIS1 C-TERMINAL PEPTIDE-BINDING DOMAIN	No other associated polymer	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

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 1C3G	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
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 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 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 oligomeric state 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
8EOD EEVD:Sis1-81 (J domain) bound conformation Deposited 2022-10-03	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–81（80 aa）	Not recorded	No recorded non-water small molecule	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

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 1–170； UniProt 180–349

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_id	1c3g
Deposition date deposition_date	1999-07-27
Structure title title	S. CEREVISIAE HEAT SHOCK PROTEIN 40 SIS1
Keywords keywords	BETA SHEETS, SHORT HELICES, CHAPERONE; CHAPERONE
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	24.19 Å
Radius of gyration Rg (electron density) rg_electron	23.89 Å
Forward intensity I(0) i0	6387980.00
Molecular weight molecular_weight	19064.0 kDa
Excluded volume excluded_volume	24085 Å³
Envelope volume envelope_volume	31266 Å³
Hydration-shell volume shell_volume	12943 Å³
Envelope diameter envelope_diameter	90.8 Å
Shell Rg shell_rg	26.65 Å
Envelope Rg envelope_rg	24.85 Å
Shape Rg shape_rg	23.89 Å
Total Rg total_rg	24.32 Å
Total atoms total_atoms	1346
Residues n_residues	170
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	91.1 Å
Rg (real space) rg_real	24.75 Å
Rg uncertainty (real space) rg_real_error	1.04 Å
I(0) (real space) i0_real	6.3880e+06
I(0) uncertainty (real space) i0_real_error	9.9420e+04
Rg (reciprocal space) rg_reciprocal	24.62 Å
I(0) (reciprocal space) i0_reciprocal	6387000.0000
Solution quality estimate total_estimate	0.7043
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	18.5 Å
Skewness Skewness skewness	0.664
Kurtosis Kurtosis kurtosis	-0.203
Angular range angular_range	— – 0.3300 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	761300.0000
Real-space data points n_real_points	65
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.384; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.078; Smooth: 0.921

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1c3ga1
Class class	b — All beta proteins
Fold Fold fold	b.4 — HSP40/DnaJ peptide-binding domain
Superfamily Superfamily superfamily	b.4.1 — HSP40/DnaJ peptide-binding domain
Family Family family	b.4.1.1 — HSP40/DnaJ peptide-binding domain

Domain ID domain_id	d1c3ga2
Class class	b — All beta proteins
Fold Fold fold	b.4 — HSP40/DnaJ peptide-binding domain
Superfamily Superfamily superfamily	b.4.1 — HSP40/DnaJ peptide-binding domain
Family Family family	b.4.1.1 — HSP40/DnaJ peptide-binding domain

CATH v4.4 (2 domains)

Domain ID domain_id	1c3gA01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	260 — HSP40/DNAj peptide-binding domain
Homologous superfamily homologous superfamily	20 — Urease metallochaperone UreE, N-terminal domain

Domain ID domain_id	1c3gA02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	260 — HSP40/DNAj peptide-binding domain
Homologous superfamily homologous superfamily	20 — Urease metallochaperone UreE, N-terminal domain

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8. Citations (1)

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Unit-cell length a length_a	73.420 Å
Unit-cell length b length_b	73.420 Å
Unit-cell length c length_c	80.090 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 41 21 2
Space-group number int_tables_number	92
Crystal system crystal_system	—

Resolution resolution	2.700 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.2650
R_work r_work	0.2650
R_free r_free	0.3110

Description description	HEAT SHOCK PROTEIN 40
Molecular weight formula_weight	19097.8 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1379

S. CEREVISIAE HEAT SHOCK PROTEIN 40 SIS1

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

HEAT SHOCK PROTEIN 40

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Saccharomyces cerevisiae
通用名 common_name	;baker's yeast ;
NCBI Class编号 ncbi_taxonomy_id	4932
宿主生物 host_organism	Escherichia coli

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	33

fit	/app/data/saxs_computation/c3/1c3g/1c3g.fit
pddf	/app/data/pr_computation/c3/1c3g/1c3g.pr.out
profile	/app/data/saxs_computation/c3/1c3g/1c3g.dat