SAXSdb — 2bbu

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

Suppressor of cytokine signaling 3

Mus musculus

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 22–185	Fragment：KIR/ESS/SH2 DOMAIN/PEST MOTIF	GP130 PHOSPHOPEPTIDE × 1	SOLUTION NMR NMR measurement conditions：pH 6.7；298 K；Ionic strength (raw mmCIF value) 50mM；Pressure 1 NMR sample composition：0.3mM U-15N-13C-SOCS3/0.3mM phophopeptide, 20mM Na-phosphate, pH 6.7, 2mM DTT, 1mM edta, 50mM glutamate, 50mM Arginine, 5% D2O \| 95% H20, 5% D2O NMR sample composition：0.3mM U-15N-SOCS3/0.3mM phophopeptide, 20mM Na-phosphate, pH 6.7, 2mM DTT, 1mM edta, 50mM glutamate, 50mM Arginine, 5% D2O \| 95% H20, 5% D2O NMR sample composition：0.3mM U-13C-SOCS3/0.3mM phophopeptide, 20mM Na-phosphate, pH 6.7, 2mM DTT, 1mM edta, 50mM glutamate, 50mM Arginine, 5% D2O \| 95% H20, 5% D2O NMR sample composition：0.3mM SOCS3/0.3mM phophopeptide, 20mM Na-phosphate, pH 6.7, 2mM DTT, 1mM edta, 50mM glutamate, 50mM Arginine, 5% D2O \| 95% H20, 5% D2O NMR sample composition：0.3mM SOCS3/0.3mM phophopeptide, 20mM Na-phosphate, pH 6.7, 2mM DTT, 1mM edta, 50mM glutamate, 50mM Arginine, 5% D2O \| 100% 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 2BBU	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2HMH Crystal structure of SOCS3 in complex with gp130(pTyr757) phosphopeptide. Deposited 2006-07-11	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 15–130（116 aa） Chain A 154–185（32 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；297 K；30% PEG8000, 0.1 M Sodium Cacodylate, 0.2 M Sodium Acetate, VAPOR DIFFUSION, HANGING DROP, temperature 297K, pH 6.50	Resolution 2.00 Å R-free 0.291
2JZ3 SOCS box elonginBC ternary complex Deposited 2007-12-27	Different construct Different oligomeric state Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 186–225（40 aa） Fragment：SOCS box, UNP residues 186-225	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.7；310 K；Ionic strength (raw mmCIF value) 0.05；Pressure ambient NMR sample composition 1mM [U-100% 13C; U-100% 15N] socs box; 1mM elonginB; 1mM elonginC; 50mM potassium chloride; 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
4GL9 Crystal structure of inhibitory protein SOCS3 in complex with JAK2 kinase domain and fragment of GP130 intracellular domain Deposited 2012-08-14	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain E 38–128（91 aa） Fragment：chimeric fusion of Intracellular domain (unp residues 22-128 and 163-185)	Not recorded	IZA 2-TERT-BUTYL-9-FLUORO-3,6-DIHYDRO-7H-BENZ[H]-IMIDAZ[4,5-F]ISOQUINOLINE-7-ONE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.2；298 K；0.33M di-potassium hydrogen phosphate, 1.67M sodium dihydrogen phosphate, 0.1M phosphate-citrate, pH 4.2, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 3.90 Å R-free 0.281
4GL9 Crystal structure of inhibitory protein SOCS3 in complex with JAK2 kinase domain and fragment of GP130 intracellular domain Deposited 2012-08-14	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain H 38–128（91 aa） Fragment：chimeric fusion of Intracellular domain (unp residues 22-128 and 163-185)	Not recorded	IZA 2-TERT-BUTYL-9-FLUORO-3,6-DIHYDRO-7H-BENZ[H]-IMIDAZ[4,5-F]ISOQUINOLINE-7-ONE × 1 PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.2；298 K；0.33M di-potassium hydrogen phosphate, 1.67M sodium dihydrogen phosphate, 0.1M phosphate-citrate, pH 4.2, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 3.90 Å R-free 0.281
4GL9 Crystal structure of inhibitory protein SOCS3 in complex with JAK2 kinase domain and fragment of GP130 intracellular domain Deposited 2012-08-14	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain G 38–128（91 aa） Fragment：chimeric fusion of Intracellular domain (unp residues 22-128 and 163-185)	Not recorded	IZA 2-TERT-BUTYL-9-FLUORO-3,6-DIHYDRO-7H-BENZ[H]-IMIDAZ[4,5-F]ISOQUINOLINE-7-ONE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.2；298 K；0.33M di-potassium hydrogen phosphate, 1.67M sodium dihydrogen phosphate, 0.1M phosphate-citrate, pH 4.2, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 3.90 Å R-free 0.281
4GL9 Crystal structure of inhibitory protein SOCS3 in complex with JAK2 kinase domain and fragment of GP130 intracellular domain Deposited 2012-08-14	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain F 38–128（91 aa） Fragment：chimeric fusion of Intracellular domain (unp residues 22-128 and 163-185)	Not recorded	IZA 2-TERT-BUTYL-9-FLUORO-3,6-DIHYDRO-7H-BENZ[H]-IMIDAZ[4,5-F]ISOQUINOLINE-7-ONE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.2；298 K；0.33M di-potassium hydrogen phosphate, 1.67M sodium dihydrogen phosphate, 0.1M phosphate-citrate, pH 4.2, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 3.90 Å R-free 0.281

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

View Construct and Data Evidence

UniProt name	SOCS3_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–164； UniProt 22–185

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	2bbu
Deposition date deposition_date	2005-10-17
Structure title title	solution structure of mouse socs3 in complex with a phosphopeptide from the gp130 receptor
Keywords keywords	SH2 DOMAIN, EXTENDED SH2 SUBDOMAIN, PEST MOTIF, PROTEIN COMPLEX, PHOSPHOPEPTIDE, CYTOKINE REGULATOR; CYTOKINE REGULATOR
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	17.80 Å
Radius of gyration Rg (electron density) rg_electron	17.29 Å
Forward intensity I(0) i0	1980110000.00
Molecular weight molecular_weight	373380.0 kDa
Excluded volume excluded_volume	465650 Å³
Envelope volume envelope_volume	82948 Å³
Hydration-shell volume shell_volume	28995 Å³
Envelope diameter envelope_diameter	77.2 Å
Shell Rg shell_rg	31.79 Å
Envelope Rg envelope_rg	24.23 Å
Shape Rg shape_rg	17.28 Å
Total Rg total_rg	17.64 Å
Total atoms total_atoms	52020
Residues n_residues	3400
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	70.8 Å
Rg (real space) rg_real	17.86 Å
Rg uncertainty (real space) rg_real_error	0.67 Å
I(0) (real space) i0_real	1.9800e+09
I(0) uncertainty (real space) i0_real_error	2.7690e+07
Rg (reciprocal space) rg_reciprocal	17.85 Å
I(0) (reciprocal space) i0_reciprocal	1980000000.0000
Solution quality estimate total_estimate	0.7670
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	20.1 Å
Skewness Skewness skewness	0.543
Kurtosis Kurtosis kurtosis	0.194
Angular range angular_range	— – 0.4450 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	2573000.0000
Real-space data points n_real_points	75
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.401; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.766; Smooth: 0.999

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	Suppressor of cytokine signaling 3
Molecular weight formula_weight	17961.2 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	52020

LKTFSSKSEYQLVVNAVRKLQESGFYWSAVTGGEANLLLSAEPAGTFLIRDSSDQRHFFTLSVKTQSGTKNLRIQCEGGSFSLQSDPRSTQPVPRFDCVLKLVHHYMPPPGTPSFSLPPTEPSSEVPEQPPAQALPGSTPKRAYYIYSGGEKIPLVLSRPLSSN

来源 Source

来源生物 organism	Mus musculus
通用名 common_name	house mouse
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Escherichia coli BL21

Entity 2 Entity 2 polymer

Description description	GP130 PHOSPHOPEPTIDE
Molecular weight formula_weight	1605.6 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

STASTVEYSTVVHSG

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	2bbuA00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	505 — SHC Adaptor Protein
Homologous superfamily homologous superfamily	10 — SH2 domain

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8. Citations (1)

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fit	/app/data/saxs_computation/bb/2bbu/2bbu.fit
pddf	/app/data/pr_computation/bb/2bbu/2bbu.pr.out
profile	/app/data/saxs_computation/bb/2bbu/2bbu.dat

solution structure of mouse socs3 in complex with a phosphopeptide from the gp130 receptor

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

Suppressor of cytokine signaling 3

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

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)