SAXSdb — 6kzh

▼

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

14-3-3 protein theta

Homo sapiens

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 × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 2–234 Chain B； UniProt 2–234	Not recorded	CIC pS173 peptide × 2 （Q96RK0）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M Sodium chloride, 0.1 M HEPES pH 7.5, 25% w/v Polyethylene glycol 3,350	Resolution 2.65 Å R-free 0.274

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 6KZH	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2BTP 14-3-3 Protein Theta (Human) Complexed to Peptide Deposited 2005-06-05	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–234（234 aa） Chain B 1–234（234 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；0.2M SODIUM ACETATE TRIHYDRATE, 0.1M TRISHCL PH8.5,30% PEG4000, pH 8.50	Resolution 2.80 Å R-free 0.259
5IQP 14-3-3 PROTEIN TAU ISOFORM Deposited 2016-03-11	Different construct 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 1–245（245 aa） Chain B 1–245（245 aa）	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.4；291 K；24% PEG4K, 140 mM LI2SO4, 4 % of SATURATED NACL IN 80 mM MES AT pH 6.4; PROTEIN 7 mg/ml	Resolution 2.60 Å R-free 0.239
6BCR Complex of 14-3-3 theta with an IRSp53 peptide phosphorylated at T340 Deposited 2017-10-20	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–245（245 aa） Chain B 1–245（245 aa）	Not recorded	MG MAGNESIUM ION × 3 PEG DI(HYDROXYETHYL)ETHER × 2 1PE PENTAETHYLENE GLYCOL × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291.15 K；0.15 M Magnesium Formate, 18% PEG3350, 4% TFE	Resolution 1.99 Å R-free 0.229
6BCR Complex of 14-3-3 theta with an IRSp53 peptide phosphorylated at T340 Deposited 2017-10-20	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain E 1–245（245 aa） Chain F 1–245（245 aa）	Not recorded	MG MAGNESIUM ION × 2 PEG DI(HYDROXYETHYL)ETHER × 3 1PE PENTAETHYLENE GLYCOL × 1 EDO 1,2-ETHANEDIOL × 1 ETF TRIFLUOROETHANOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291.15 K；0.15 M Magnesium Formate, 18% PEG3350, 4% TFE	Resolution 1.99 Å R-free 0.229
6BD2 Complex of 14-3-3 theta with an IRSp53 peptide doubly-phosphorylated at T340 and S366 Deposited 2017-10-20	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–245（245 aa） Chain B 1–245（245 aa）	Not recorded	PEG DI(HYDROXYETHYL)ETHER × 1 1PE PENTAETHYLENE GLYCOL × 1 PG4 TETRAETHYLENE GLYCOL × 1 PGE TRIETHYLENE GLYCOL × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291.15 K；0.1 M CaCl2, 13% Peg 3350	Resolution 2.90 Å R-free 0.254
6BQT Complex of 14-3-3 theta with an IRSp53 peptide doubly-phosphorylated at T340 and T360 Deposited 2017-11-28	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–245（245 aa） Chain B 1–245（245 aa）	Not recorded	PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL × 1 1PE PENTAETHYLENE GLYCOL × 3 EDO 1,2-ETHANEDIOL × 1 PG4 TETRAETHYLENE GLYCOL × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291.15 K；0.1 M CaCl2, 13% Peg 3350	Resolution 2.80 Å R-free 0.287
6BQT Complex of 14-3-3 theta with an IRSp53 peptide doubly-phosphorylated at T340 and T360 Deposited 2017-11-28	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain D 1–245（245 aa） Chain E 1–245（245 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 1 PG4 TETRAETHYLENE GLYCOL × 2 PGE TRIETHYLENE GLYCOL × 1 PEG DI(HYDROXYETHYL)ETHER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291.15 K；0.1 M CaCl2, 13% Peg 3350	Resolution 2.80 Å R-free 0.287
6BQT Complex of 14-3-3 theta with an IRSp53 peptide doubly-phosphorylated at T340 and T360 Deposited 2017-11-28	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain G 1–245（245 aa） Chain H 1–245（245 aa）	Not recorded	1PE PENTAETHYLENE GLYCOL × 2 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291.15 K；0.1 M CaCl2, 13% Peg 3350	Resolution 2.80 Å R-free 0.287
6BQT Complex of 14-3-3 theta with an IRSp53 peptide doubly-phosphorylated at T340 and T360 Deposited 2017-11-28	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain J 1–245（245 aa） Chain K 1–245（245 aa）	Not recorded	1PE PENTAETHYLENE GLYCOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291.15 K；0.1 M CaCl2, 13% Peg 3350	Resolution 2.80 Å R-free 0.287
6KZG 14-3-3 protein in Complex with CIC S301 phosphorylated peptide Deposited 2019-09-24	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 2–234（233 aa） Chain B 2–234（233 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；293 K；8% v/v TacsimateTM pH 6.0, 20% w/v Polyethylene glycol 3350	Resolution 2.00 Å R-free 0.231
7QI1 Crystal structure of human 14-3-3 protein beta in complex with CFTR peptide pS753pS768 and PPI stabilizer CY007424 Deposited 2021-12-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: octameric	Chain A 1–230（230 aa） Chain B 1–230（230 aa） Chain C 1–230（230 aa） Chain D 1–230（230 aa）	Not recorded	ARG ARGININE × 2 Q95 [2-(2-methylphenyl)sulfanylphenyl]methanamine × 2 TYR TYROSINE × 2 GLN GLUTAMINE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；Qiagen Cryos Suite #44 (0.09 M HEPES sodium salt pH7.5, 1.26M tri-sodium citrate, 10% (v/v) glycerol) with an extra 2% (v/v) of glycerol.	Resolution 1.76 Å R-free 0.241

7 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	1433T_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 31–263； UniProt 2–234 Author chain B； PDBConstruct 31–263； UniProt 2–234

CIC pS173 peptide

Homo sapiens

UniProt Q96RK0

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 × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain C； UniProt 170–177 Chain Q； UniProt 170–177	Non-standard monomer：Yes (specific site not provided by mmCIF)	14-3-3 protein theta × 2 （P27348）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M Sodium chloride, 0.1 M HEPES pH 7.5, 25% w/v Polyethylene glycol 3,350	Resolution 2.65 Å R-free 0.274

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 6KZH	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2M41 Solution Structure of the AXH domain of Ataxin-1 in complex with ligand peptide from Capicua Deposited 2013-01-28	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 34–48（15 aa） Fragment：Ataxin-1-binding linear motif (UNP 34-48)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.8；310 K；Ionic strength (raw mmCIF value) 20；Pressure ambient NMR sample composition 0.5 mM [U-100% 13C; U-100% 15N] Ataxin-1 AXH domain, 0.6 mM CIC polypeptide, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.5 mM [U-100% 15N] Ataxin-1 AXH domain, 0.6 mM CIC polypeptide, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
4J2J Crystal structure of AXH domain complex with Capicua Deposited 2013-02-04	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 28–48（21 aa） Fragment：UNP residues 28-48	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；0.1M Calcium chloride, 24%(v/v) PEG3350, 4%(v/v) pentaerythritol ethoxylate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å R-free 0.270
4J2J Crystal structure of AXH domain complex with Capicua Deposited 2013-02-04	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 28–48（21 aa） Fragment：UNP residues 28-48	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；0.1M Calcium chloride, 24%(v/v) PEG3350, 4%(v/v) pentaerythritol ethoxylate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å R-free 0.270
4J2J Crystal structure of AXH domain complex with Capicua Deposited 2013-02-04	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 28–48（21 aa） Fragment：UNP residues 28-48	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；0.1M Calcium chloride, 24%(v/v) PEG3350, 4%(v/v) pentaerythritol ethoxylate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å R-free 0.270
4J2L Crystal Structure of AXH domain complexed with Capicua Deposited 2013-02-04	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 21–48（28 aa） Fragment：UNP residues 21-48	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；1.6M NaCl, 3%(v/v) glycerol, 16%(w/v) PEG3350, 1mM L-Glutathione, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.15 Å R-free 0.294
4J2L Crystal Structure of AXH domain complexed with Capicua Deposited 2013-02-04	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 21–48（28 aa） Fragment：UNP residues 21-48	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；1.6M NaCl, 3%(v/v) glycerol, 16%(w/v) PEG3350, 1mM L-Glutathione, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.15 Å R-free 0.294
6JRP Crystal structure of CIC-HMG-ETV5-DNA complex Deposited 2019-04-05	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: trimeric	Chain A 199–276（78 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；Ammonium acetate, PEG3350, Bis-tris pH 6.5	Resolution 3.00 Å R-free 0.334
6JRP Crystal structure of CIC-HMG-ETV5-DNA complex Deposited 2019-04-05	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein–DNA Monomer；Protein × 1 PDB declaration: trimeric	Chain D 199–276（78 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；Ammonium acetate, PEG3350, Bis-tris pH 6.5	Resolution 3.00 Å R-free 0.334
6JRP Crystal structure of CIC-HMG-ETV5-DNA complex Deposited 2019-04-05	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein–DNA Monomer；Protein × 1 PDB declaration: trimeric	Chain G 199–276（78 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；Ammonium acetate, PEG3350, Bis-tris pH 6.5	Resolution 3.00 Å R-free 0.334
6JRP Crystal structure of CIC-HMG-ETV5-DNA complex Deposited 2019-04-05	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein–DNA Monomer；Protein × 1 PDB declaration: trimeric	Chain J 199–276（78 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；Ammonium acetate, PEG3350, Bis-tris pH 6.5	Resolution 3.00 Å R-free 0.334
6KZG 14-3-3 protein in Complex with CIC S301 phosphorylated peptide Deposited 2019-09-24	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 298–305（8 aa） Chain Q 298–305（8 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 VAPOR DIFFUSION, SITTING DROP；pH 6；293 K；8% v/v TacsimateTM pH 6.0, 20% w/v Polyethylene glycol 3350	Resolution 2.00 Å R-free 0.231
7M5W Crystal structure of the HMG-C1 domain of human capicua bound to DNA Deposited 2021-03-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: trimeric	Chain A 188–280（93 aa） Fragment：HMG box domain UNP residues 188-280 fused with C1 domain UNP residues 1457-1527 Chain A 1457–1527（71 aa） Fragment：HMG box domain UNP residues 188-280 fused with C1 domain UNP residues 1457-1527	Not recorded	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；291 K；100 mM MES, 100 mM CaCl2, 100 mM NaCl, and 16% (w/v) PEG 8000	Resolution 2.95 Å R-free 0.243

6 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CIC_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–8； UniProt 170–177 Author chain Q； PDBConstruct 1–8； UniProt 170–177

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	6kzh
Deposition date deposition_date	2019-09-24
Structure title title	14-3-3 protein in Complex with CIC S173 phosphorylated peptide
Keywords keywords	14-3-3 protein, CIC, phosphorylation, transcriptional regulation, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method method	X-RAY DIFFRACTION

▼

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

Radius of gyration Rg (Guinier) rg_guinier	27.47 Å
Radius of gyration Rg (electron density) rg_electron	26.63 Å
Forward intensity I(0) i0	48099500.00
Molecular weight molecular_weight	53098.0 kDa
Excluded volume excluded_volume	66240 Å³
Envelope volume envelope_volume	85394 Å³
Hydration-shell volume shell_volume	26831 Å³
Envelope diameter envelope_diameter	84.5 Å
Shell Rg shell_rg	33.86 Å
Envelope Rg envelope_rg	26.12 Å
Shape Rg shape_rg	26.64 Å
Total Rg total_rg	27.39 Å
Total atoms total_atoms	3723
Residues n_residues	469
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

▼

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

Maximum dimension Dmax dmax	83.9 Å
Rg (real space) rg_real	27.41 Å
Rg uncertainty (real space) rg_real_error	0.56 Å
I(0) (real space) i0_real	4.8100e+07
I(0) uncertainty (real space) i0_real_error	7.3450e+05
Rg (reciprocal space) rg_reciprocal	27.43 Å
I(0) (reciprocal space) i0_reciprocal	48100000.0000
Solution quality estimate total_estimate	0.9148
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	31.8 Å
Skewness Skewness skewness	0.174
Kurtosis Kurtosis kurtosis	-0.710
Angular range angular_range	— – 0.2900 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	7802000.0000
Real-space data points n_real_points	59
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.979; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.958

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	14-3-3 protein theta
Molecular weight formula_weight	29857.6 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	3723

MGSSHHHHHHSSGLVPRGSHMASENLYFQGEKTELIQKAKLAEQAERYDDMATCMKAVTEQGAELSNEERNLLSVAYKNVVGGRRSAWRVISSIEQKTDTSDKKLQLIKDYREKVESELRSICTTVLELLDKYLIANATNPESKVFYLKMKGDYFRYLAEVACGDDRKQTIDNSQGAYQEAFDISKKEMQPTHPIRLGLALNFSVFYYEILNNPELACTLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDSAG

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	Human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 polymer

Description description	CIC pS173 peptide
Molecular weight formula_weight	956.0 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,Q

RTQSLSAL

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	Human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli BL21(DE3)

▼

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d6kzha1
Class class	a — All alpha proteins
Fold Fold fold	a.118 — alpha-alpha superhelix
Superfamily Superfamily superfamily	a.118.7 — 14-3-3 protein
Family Family family	a.118.7.1 — 14-3-3 protein

Domain ID domain_id	d6kzha2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d6kzhb1
Class class	a — All alpha proteins
Fold Fold fold	a.118 — alpha-alpha superhelix
Superfamily Superfamily superfamily	a.118.7 — 14-3-3 protein
Family Family family	a.118.7.1 — 14-3-3 protein

Domain ID domain_id	d6kzhb2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

▶

8. Citations (1)

▶

Unit-cell length a length_a	70.169 Å
Unit-cell length b length_b	80.810 Å
Unit-cell length c length_c	107.064 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 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.645 Å
Low-resolution limit resolution_low	44.628 Å
R factor r_factor	0.2212
R_work r_work	0.2154
R_free r_free	0.2736

fit	/app/data/saxs_computation/kz/6kzh/6kzh.fit
pddf	/app/data/pr_computation/kz/6kzh/6kzh.pr.out
profile	/app/data/saxs_computation/kz/6kzh/6kzh.dat

14-3-3 protein in Complex with CIC S173 phosphorylated peptide

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

14-3-3 protein theta

State in the Current Structure

Other States of the Same Protein in the Database

CIC pS173 peptide

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 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)