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3cwg

Unphosphorylated mouse STAT3 core fragment

Method: X-RAY DIFFRACTION Dmax: 134.6 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Signal transducer and activator of transcription 3

Mus musculus

UniProt P42227

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 127–688 Fragment：STAT3 Core Fragment, UNP residues (127-688) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5.7；277 K；0.1M Bis-tris, 0.5M ammonium sulfate, 12% PEG3350, 0.1mM KCl, 0.05M NaI, pH 5.7, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.05 Å R-free 0.269
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain B； UniProt 127–688 Fragment：STAT3 Core Fragment, UNP residues (127-688) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5.7；277 K；0.1M Bis-tris, 0.5M ammonium sulfate, 12% PEG3350, 0.1mM KCl, 0.05M NaI, pH 5.7, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.05 Å R-free 0.269

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 3CWG Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1BG1 TRANSCRIPTION FACTOR STAT3B/DNA COMPLEX Deposited 1998-06-03 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 127–722（596 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；pH 7.0
Resolution 2.25 Å R-free 0.301
4E68 Unphosphorylated STAT3B core protein binding to dsDNA Deposited 2012-03-15 Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 127–722（596 aa） Fragment：STAT3 Core Fragment, residues (127-722)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；277 K；0.005M MgSO4, 0.1M ammonium acetate, 10% glycerol, 0.05M MES pH 5.6, 0.25M NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.58 Å R-free 0.273
4ZIA Crystal Structure of STAT3 N-terminal domain Deposited 2015-04-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 3–127（125 aa） Fragment：N-terminal domain (UNP residues 3-127)
Chain B 3–127（125 aa） Fragment：N-terminal domain (UNP residues 3-127)
Not recorded NI NICKEL (II) ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；20% v/v PEG 3350, 0.2M magnesium formate
Resolution 2.70 Å R-free 0.270
4ZIA Crystal Structure of STAT3 N-terminal domain Deposited 2015-04-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 3–127（125 aa） Fragment：N-terminal domain (UNP residues 3-127)
Chain D 3–127（125 aa） Fragment：N-terminal domain (UNP residues 3-127)
Not recorded FMT FORMIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；20% v/v PEG 3350, 0.2M magnesium formate
Resolution 2.70 Å R-free 0.270
4ZIA Crystal Structure of STAT3 N-terminal domain Deposited 2015-04-28 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain E 3–127（125 aa） Fragment：N-terminal domain (UNP residues 3-127)
Not recorded MG MAGNESIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；20% v/v PEG 3350, 0.2M magnesium formate
Resolution 2.70 Å R-free 0.270

3 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name STAT3_MOUSE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–562； UniProt 127–688 Author chain B； PDBConstruct 1–562； UniProt 127–688

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 3cwg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3cwg
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3cwg
Deposition date deposition_date2008-04-21
Structure title titleUnphosphorylated mouse STAT3 core fragment
Keywords keywords;STAT3, Activator, Acute phase, Alternative splicing, Cytoplasm, DNA-binding, Nucleus, Phosphoprotein, SH2 domain, Transcription, Transcription regulation ;; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier41.54 Å
Radius of gyration Rg (electron density) rg_electron40.98 Å
Forward intensity I(0) i0193819000.00
Molecular weight molecular_weight116950.0 kDa
Excluded volume excluded_volume147880 ų
Envelope volume envelope_volume205890 ų
Hydration-shell volume shell_volume41696 ų
Envelope diameter envelope_diameter142.0 Å
Shell Rg shell_rg46.95 Å
Envelope Rg envelope_rg40.26 Å
Shape Rg shape_rg40.94 Å
Total Rg total_rg41.48 Å
Total atoms total_atoms8215
Residues n_residues1008
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 dmax134.6 Å
Rg (real space) rg_real41.50 Å
Rg uncertainty (real space) rg_real_error1.27 Å
I(0) (real space) i0_real1.9380e+08
I(0) uncertainty (real space) i0_real_error3.6840e+06
Rg (reciprocal space) rg_reciprocal41.54 Å
I(0) (reciprocal space) i0_reciprocal193800000.0000
Solution quality estimate total_estimate0.8889
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary60.2 Å
Skewness Skewness skewness0.133
Kurtosis Kurtosis kurtosis-0.638
Angular range angular_range— – 0.1900 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13960000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.901; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.864
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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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7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id3cwgA01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1050 — Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2
Homologous superfamily homologous superfamily20 — STAT transcription factor, all-alpha domain
Domain ID domain_id3cwgA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily630 — STAT transcription factor, DNA-binding domain
Domain ID domain_id3cwgA03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id3cwgA04
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology505 — SHC Adaptor Protein
Homologous superfamily homologous superfamily10 — SH2 domain
Domain ID domain_id3cwgB01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1050 — Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2
Homologous superfamily homologous superfamily20 — STAT transcription factor, all-alpha domain
Domain ID domain_id3cwgB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily630 — STAT transcription factor, DNA-binding domain
Domain ID domain_id3cwgB03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id3cwgB04
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology505 — SHC Adaptor Protein
Homologous superfamily homologous superfamily10 — SH2 domain
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8. Citations (1)

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9. Files and Curves (10)