SAXSdb — 8dp5

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

Protein PEAK3

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 × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain A； UniProt 1–473 Chain B； UniProt 1–473 Chain E； UniProt 1–473 Chain P； UniProt 1–473	Non-standard monomer：Yes (specific site not provided by mmCIF)	14-3-3 protein beta/alpha × 1 （P31946） 14-3-3 protein epsilon × 1 （P62258）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5；A final concentration of 0.1% of Octyl-beta-Glucoside (C14H28O6) was added to the sample before freezing. cryo-EM vitrification conditions：Cryogen ETHANE；blot time = 7s blot force = 4	Resolution 3.10 Å

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 8DP5	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
8DS6 Structure of the PEAK3 pseudokinase homodimer Deposited 2022-07-21	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–473（473 aa） Chain B 1–473（473 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；A final concentration of 0.1% of Octyl-beta-Glucoside (C14H28O6) was added to the sample before freezing. cryo-EM vitrification conditions Cryogen ETHANE；blot time = 7s blot force = 4	Resolution 4.90 Å

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	PEAK3_HUMAN
Isoform	—
PDB entities	1, 4
Chains and sequence ranges	Author chain A； PDBConstruct 1–473； UniProt 1–473 Author chain B； PDBConstruct 1–473； UniProt 1–473 Author chain E； PDBConstruct 1–473； UniProt 1–473 Author chain P； PDBConstruct 1–473； UniProt 1–473

14-3-3 protein beta/alpha

Homo sapiens

UniProt P31946

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 × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain C； UniProt 1–246	Not recorded	Protein PEAK3 × 2 （Q6ZS72） 14-3-3 protein epsilon × 1 （P62258） Protein PEAK3 fragment × 2 （Q6ZS72）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5；A final concentration of 0.1% of Octyl-beta-Glucoside (C14H28O6) was added to the sample before freezing. cryo-EM vitrification conditions：Cryogen ETHANE；blot time = 7s blot force = 4	Resolution 3.10 Å

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 8DP5	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2BQ0 14-3-3 Protein Beta (Human) Deposited 2005-04-26	Different construct Different mutation/modification 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 1–238（238 aa） Chain B 1–238（238 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；0.05M MGCL2,0.1M HEPES PH7.5, 30% PEG MME 550, pH 8.00	Resolution 2.50 Å R-free 0.273
2BQ0 14-3-3 Protein Beta (Human) Deposited 2005-04-26	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–238（238 aa） Chain B 1–238（238 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；0.05M MGCL2,0.1M HEPES PH7.5, 30% PEG MME 550, pH 8.00	Resolution 2.50 Å R-free 0.273
2C23 14-3-3 Protein Beta (Human) in complex with exoenzyme S peptide Deposited 2005-09-26	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–238（238 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；0.05M MGCL2,0.1M HEPES PH7.5, 30% PEG MME 550, pH 8.00	Resolution 2.65 Å R-free 0.286
4DNK Crystal structure of a tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, beta polypeptide (YWHAB) from homo sapiens at 2.20 A resolution. Deposited 2012-02-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–246（246 aa） Chain B 1–246（246 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	PO4 PHOSPHATE ION × 3 EDO 1,2-ETHANEDIOL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；20.00% polyethylene glycol 3350, 0.20M magnesium acetate, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.20 Å R-free 0.226
5N10 Cucurbit[8]uril and 14-3-3 based binary bivalent supramolecular-protein assembly platform Deposited 2017-02-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–246（246 aa） Chain B 1–246（246 aa）	Not recorded	GOL GLYCEROL × 1 C8L Cucurbit[8]uril × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；277.15 K；PEG 1500, sodium citrate	Resolution 1.60 Å R-free 0.194
6A5Q Structure of 14-3-3 beta in complex with TFEB 14-3-3 binding motif Deposited 2018-06-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–246（246 aa） Chain B 1–246（246 aa）	Not recorded	MLA MALONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 4；289 K；0.1 M sodium malonate, and 12% (w/v) PEG 3350	Resolution 2.00 Å R-free 0.230
6A5Q Structure of 14-3-3 beta in complex with TFEB 14-3-3 binding motif Deposited 2018-06-25	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–246（246 aa）	Not recorded	MLA MALONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 4；289 K；0.1 M sodium malonate, and 12% (w/v) PEG 3350	Resolution 2.00 Å R-free 0.230
6BYK Structure of 14-3-3 beta/alpha bound to O-ClcNAc peptide Deposited 2017-12-20	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 3–232（230 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；30% PEG 4000, 200 mM sodium acetate, 0.1 M Tris pH 8.5	Resolution 3.00 Å R-free 0.268
6BYK Structure of 14-3-3 beta/alpha bound to O-ClcNAc peptide Deposited 2017-12-20	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 3–232（230 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；30% PEG 4000, 200 mM sodium acetate, 0.1 M Tris pH 8.5	Resolution 3.00 Å R-free 0.268
6BYK Structure of 14-3-3 beta/alpha bound to O-ClcNAc peptide Deposited 2017-12-20	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 3–232（230 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；30% PEG 4000, 200 mM sodium acetate, 0.1 M Tris pH 8.5	Resolution 3.00 Å R-free 0.268
6BYK Structure of 14-3-3 beta/alpha bound to O-ClcNAc peptide Deposited 2017-12-20	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 3–232（230 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；30% PEG 4000, 200 mM sodium acetate, 0.1 M Tris pH 8.5	Resolution 3.00 Å R-free 0.268
6GN0 Exoenzyme S from Pseudomonas aeruginosa in complex with human 14-3-3 protein beta, tetrameric crystal form Deposited 2018-05-29	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–239（239 aa） Chain B 1–239（239 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；277 K；12% PEG 3350, 4% Tacsimate	Resolution 3.24 Å R-free 0.294
6GN0 Exoenzyme S from Pseudomonas aeruginosa in complex with human 14-3-3 protein beta, tetrameric crystal form Deposited 2018-05-29	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–239（239 aa） Chain D 1–239（239 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；277 K；12% PEG 3350, 4% Tacsimate	Resolution 3.24 Å R-free 0.294
6GN8 Exoenzyme S from Pseudomonas aeruginosa in complex with human 14-3-3 protein beta, trimeric crystal form Deposited 2018-05-30	Different construct Different mutation/modification 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 A 1–234（234 aa） Chain B 1–234（234 aa）	Not recorded	MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；40% MPD, 8% PEG 8000, 0.1M Sodium Cacodylate	Resolution 2.34 Å R-free 0.248
6GNJ Exoenzyme S from Pseudomonas aeruginosa in complex with human 14-3-3 protein beta, trimeric crystal form in complex with STO1101 Deposited 2018-05-31	Different construct Different mutation/modification 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 A 1–234（234 aa） Chain B 1–234（234 aa）	Not recorded	F4W 3-(12-oxidanylidene-7-thia-9,11-diazatricyclo[6.4.0.0^{2,6}]dodeca-1(8),2(6),9-trien-10-yl)propanoic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；40% MPD, 7% PEG 8000, 0.1M Sodium Cacodylate	Resolution 3.24 Å R-free 0.221
6GNK Exoenzyme S from Pseudomonas aeruginosa in complex with human 14-3-3 protein beta, trimeric crystal form bound to Carba-NAD Deposited 2018-05-31	Different construct Different mutation/modification 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 A 1–234（234 aa） Chain B 1–234（234 aa）	Not recorded	CNA CARBA-NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；50% MPD, 8% PEG 8000, 0.1M Sodium Cacodylate	Resolution 2.55 Å R-free 0.239
6GNN Exoenzyme T from Pseudomonas aeruginosa in complex with human 14-3-3 protein beta, tetrameric crystal form bound to STO1101 Deposited 2018-05-31	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–239（239 aa）	Not recorded	F4W 3-(12-oxidanylidene-7-thia-9,11-diazatricyclo[6.4.0.0^{2,6}]dodeca-1(8),2(6),9-trien-10-yl)propanoic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；293 K；12% PEG 6000, 0.1M Citrate	Resolution 3.79 Å R-free 0.385
6HEP Crystal structure of human 14-3-3 beta in complex with CFTR R-domain peptide pS753-pS768 Deposited 2018-08-20	Different construct Different mutation/modification 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 A 1–232（232 aa） Chain B 1–232（232 aa）	Not recorded	ETE 2-{2-[2-2-(METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；278 K；0.1M Tris, 25% v/v PEG350 MME	Resolution 1.86 Å R-free 0.251
6HEP Crystal structure of human 14-3-3 beta in complex with CFTR R-domain peptide pS753-pS768 Deposited 2018-08-20	Different construct Different mutation/modification 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 C 1–232（232 aa） Chain D 1–232（232 aa）	Not recorded	ETE 2-{2-[2-2-(METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；278 K；0.1M Tris, 25% v/v PEG350 MME	Resolution 1.86 Å R-free 0.251
6YGJ small-molecule stabilizer of 14-3-3 and the Carbohydrate Response Element Binding Protein (ChREBP) protein-protein interaction Deposited 2020-03-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 4–232（229 aa） Chain F 2–232（231 aa）	Not recorded	OQE [2-[2-oxidanylidene-2-(2-phenylethylamino)ethoxy]phenyl]phosphonic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；0.1M HEPES (pH 7.1), 30% MPD, 1% PEG 4000, 0.1 M Ni(II)Cl 6H2O	Resolution 2.07 Å R-free 0.277
8EQ8 The crystal structure of 14-3-3 Beta containing 3-nitrotyrosine at position Y130 Deposited 2022-10-07	Different construct Different mutation/modification 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 1–239（239 aa） Chain B 1–239（239 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, HANGING DROP；293 K；20%-30% PEG 550 MME, 50 mM MgCl2, 100 mM HEPES pH 7-8.3	Resolution 1.50 Å R-free 0.205
8EQH The crystal structure of 14-3-3 Beta containing 3-nitrotyrosine at position Y213 Deposited 2022-10-07	Different construct Different mutation/modification 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 1–239（239 aa） Chain B 1–239（239 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, HANGING DROP；293 K；20%-27% PEG 3350, +/- 50 mM MgCl2, 100 mM Bis-Tris pH 5.5-6.5	Resolution 1.90 Å R-free 0.218
9GCP ChREBP/14-3-3 complex stabilized by AMP Deposited 2024-08-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 3–232（230 aa） Chain E 3–232（230 aa）	Not recorded	AMP ADENOSINE MONOPHOSPHATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；50 mM MES ph 6.0 2.2M Sodium Malonate	Resolution 2.59 Å R-free 0.271
9GCP ChREBP/14-3-3 complex stabilized by AMP Deposited 2024-08-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 3–232（230 aa） Chain G 3–232（230 aa）	Not recorded	AMP ADENOSINE MONOPHOSPHATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；50 mM MES ph 6.0 2.2M Sodium Malonate	Resolution 2.59 Å R-free 0.271

16 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	1433B_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–246； UniProt 1–246

14-3-3 protein epsilon

Homo sapiens

UniProt P62258

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 × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain D； UniProt 1–255	Not recorded	Protein PEAK3 × 2 （Q6ZS72） 14-3-3 protein beta/alpha × 1 （P31946） Protein PEAK3 fragment × 2 （Q6ZS72）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5；A final concentration of 0.1% of Octyl-beta-Glucoside (C14H28O6) was added to the sample before freezing. cryo-EM vitrification conditions：Cryogen ETHANE；blot time = 7s blot force = 4	Resolution 3.10 Å

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 8DP5	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2BR9 14-3-3 Protein Epsilon (Human) Complexed to Peptide Deposited 2005-05-03	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–233（233 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；40% MPD, 5% PEG10000, 0.1M CACODYLATE PH6.5. PROTEIN IN 150MM NACL, 50MM TRIS PH8, pH 8.00	Resolution 1.75 Å R-free 0.239
3UAL Crystal Structure of 14-3-3 epsilon with Mlf1 peptide Deposited 2011-10-21	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–232（232 aa） Fragment：UNP residues 1-232	Not recorded	TBU TERTIARY-BUTYL ALCOHOL × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；277 K；0.1 M Na-Citrate, 35% tert-butanol, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.80 Å R-free 0.222
3UAL Crystal Structure of 14-3-3 epsilon with Mlf1 peptide Deposited 2011-10-21	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–232（232 aa） Fragment：UNP residues 1-232	Not recorded	TBU TERTIARY-BUTYL ALCOHOL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；277 K；0.1 M Na-Citrate, 35% tert-butanol, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.80 Å R-free 0.222
3UBW Complex of 14-3-3 isoform epsilon, a Mlf1 phosphopeptide and a small fragment hit from a FBDD screen Deposited 2011-10-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–234（234 aa） Fragment：delta C, UNP residues 1-234	Non-standard monomer：Yes (specific site not provided by mmCIF)	TBU TERTIARY-BUTYL ALCOHOL × 10 6SP (3S)-pyrrolidin-3-ol × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；277 K；For crystallization of the 14-3-3 /MLF129-42 peptide complex, protein and peptide were mixed in a 1:1.5 molar ratio in 20 mM Hepes/NaOH pH 7.5, 2 mM MgCl2 and 2 mM 2-ME and set up for crystallization in 0.1 M Na-Citrate pH 5.6 and 35% tert-butanol at 4 C, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.90 Å R-free 0.238
3UBW Complex of 14-3-3 isoform epsilon, a Mlf1 phosphopeptide and a small fragment hit from a FBDD screen Deposited 2011-10-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–234（234 aa） Fragment：delta C, UNP residues 1-234	Non-standard monomer：Yes (specific site not provided by mmCIF)	TBU TERTIARY-BUTYL ALCOHOL × 5 6SP (3S)-pyrrolidin-3-ol × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；277 K；For crystallization of the 14-3-3 /MLF129-42 peptide complex, protein and peptide were mixed in a 1:1.5 molar ratio in 20 mM Hepes/NaOH pH 7.5, 2 mM MgCl2 and 2 mM 2-ME and set up for crystallization in 0.1 M Na-Citrate pH 5.6 and 35% tert-butanol at 4 C, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.90 Å R-free 0.238
6EIH The crystal structure of 14-3-3 epsilon in complex with the phosphorylated NELFE peptide Deposited 2017-09-19	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 3–232（230 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；40% pentaerythritol propoxylate, 0.2M sodium thiocyanate, 0.1M HEPES, pH 7.0	Resolution 2.70 Å R-free 0.241
7C8E Crystal Structure of 14-3-3 epsilon with 9J10 peptide Deposited 2020-05-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–232（232 aa） Chain B 1–232（232 aa）	Not recorded	TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；289.15 K；28% PEG 400, 0.1M Hepes pH 7.5, 0.2M Calcium chloride	Resolution 3.16 Å R-free 0.271
8DGM 14-3-3 epsilon bound to phosphorylated PEAK1 (pT1165) peptide Deposited 2022-06-24	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–255（255 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；1.8 M ammonium sulfate, 0.1 M HEPES pH 7.5, 5% (v/v) MPD	Resolution 3.20 Å R-free 0.266
8DGN 14-3-3 epsilon bound to phosphorylated PEAK2 (pS826) peptide Deposited 2022-06-24	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 1–255（255 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；1.8 M ammonium sulfate, 0.1 M HEPES pH 7.5, 5% (v/v) MPD	Resolution 3.16 Å R-free 0.295
8DGP 14-3-3 epsilon bound to phosphorylated PEAK3 (pS69) peptide Deposited 2022-06-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–255（255 aa） Chain B 1–255（255 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 2 SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9.35；293 K；2M ammonium sulfate, 0.1 M sodium bicine pH 9.35, 5% (v/v) 2-methyl-2,4,-pentandiol (MPD)	Resolution 2.70 Å R-free 0.233
8DGP 14-3-3 epsilon bound to phosphorylated PEAK3 (pS69) peptide Deposited 2022-06-24	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–255（255 aa） Chain D 1–255（255 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9.35；293 K；2M ammonium sulfate, 0.1 M sodium bicine pH 9.35, 5% (v/v) 2-methyl-2,4,-pentandiol (MPD)	Resolution 2.70 Å R-free 0.233
8Q1S Pathogenic mutations of human phosphorylation sites affect protein-protein interactions Deposited 2023-08-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–255（255 aa） Chain B 1–255（255 aa）	Not recorded	BR BROMIDE ION × 1 EDO 1,2-ETHANEDIOL × 2 NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；19% PEG 3350, 0.35 M NaBr, 0.1 M BisTris-Propane pH 6.5	Resolution 3.23 Å R-free 0.279

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

View Construct and Data Evidence

UniProt name	1433E_HUMAN
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain D； PDBConstruct 1–255； UniProt 1–255

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	8dp5
Deposition date deposition_date	2022-07-14
Structure title title	Structure of the PEAK3/14-3-3 complex
Keywords keywords	complex, pseudokinase, kinase, adapter, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	42.79 Å
Radius of gyration Rg (electron density) rg_electron	42.79 Å
Forward intensity I(0) i0	238468000.00
Molecular weight molecular_weight	125960.0 kDa
Excluded volume excluded_volume	158200 Å³
Envelope volume envelope_volume	238440 Å³
Hydration-shell volume shell_volume	49815 Å³
Envelope diameter envelope_diameter	146.3 Å
Shell Rg shell_rg	44.14 Å
Envelope Rg envelope_rg	41.65 Å
Shape Rg shape_rg	42.80 Å
Total Rg total_rg	42.81 Å
Total atoms total_atoms	17780
Residues n_residues	1143
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	148.7 Å
Rg (real space) rg_real	42.98 Å
Rg uncertainty (real space) rg_real_error	1.72 Å
I(0) (real space) i0_real	2.3850e+08
I(0) uncertainty (real space) i0_real_error	4.2280e+06
Rg (reciprocal space) rg_reciprocal	42.79 Å
I(0) (reciprocal space) i0_reciprocal	238400000.0000
Solution quality estimate total_estimate	0.8613
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	40.2 Å
Skewness Skewness skewness	0.378
Kurtosis Kurtosis kurtosis	-0.528
Angular range angular_range	— – 0.1850 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	24460000.0000
Real-space data points n_real_points	38
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.820; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.878; Smooth: 0.854

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Protein PEAK3
Molecular weight formula_weight	52357.0 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	17780

MSSPEPPTEPPEPDNPTWSTQPTYSNLGQIRAHLLPSKACRLRTPGSLSTNPEPLPPPLPKKILTRTQSLPTRRTLHPSSIQVQPPRRPFLGSHSVDKSQAAVGPACLPAELTFGPADAPLGLSLRDLHSPEAVHTALAARQLQGLRTIYARLRARLMGGHPGPCHPGHSFRLLDSSPCAESGDALYYRVVRAHEDAWHILVAKVPKPGADVPHPWGLELQASLSPHFNLQGLCGLVPEGTLPGAPWRGAVALAAEVPERTVAQWLAEACTQPPEEFVWAVALLLLQLSAALKFLEAWGAALVELRPENLLLVAPRGCATTGPPRLLLTDFGRVCLQPPGPPGSPGPHAPQLGSLLRALLSLAAPSTTPLAAGLELLAAQLTRLRPSASRTRGALQALLWGPGPELRGRGAPLGPWLRALGPWLRVRRGLLVLRLAERAAGGEAPSLEDWLCCEYLAEATESSMGQALALLWDLEGGGGADYKDDDDKGPV

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	Homo sapiens

Entity 2 Entity 2 polymer

Description description	14-3-3 protein beta/alpha
Molecular weight formula_weight	28114.4 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

MTMDKSELVQKAKLAEQAERYDDMAAAMKAVTEQGHELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTERNEKKQQMGKEYREKIEAELQDICNDVLELLDKYLIPNATQPESKVFYLKMKGDYFRYLSEVASGDNKQTTVSNSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTSENQGDEGDAGEGEN

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	Homo sapiens

Entity 3 Entity 3 polymer

Description description	14-3-3 protein epsilon
Molecular weight formula_weight	29208.9 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D

MDDREDLVYQAKLAEQAERYDEMVESMKKVAGMDVELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEENKGGEDKLKMIREYRQMVETELKLICCDILDVLDKHLIPAANTGESKVFYYKMKGDYHRYLAEFATGNDRKEAAENSLVAYKAASDIAMTELPPTHPIRLGLALNFSVFYYEILNSPDRACRLAKAAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDMQGDGEEQNKEALQDVEDENQ

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	Homo sapiens

Entity 4 Entity 4 polymer

Description description	Protein PEAK3 fragment
Molecular weight formula_weight	52437.0 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,P

MSSPEPPTEPPEPDNPTWSTQPTYSNLGQIRAHLLPSKACRLRTPGSLSTNPEPLPPPLPKKILTRTQSLPTRRTLHPSSIQVQPPRRPFLGSHSVDKSQAAVGPACLPAELTFGPADAPLGLSLRDLHSPEAVHTALAARQLQGLRTIYARLRARLMGGHPGPCHPGHSFRLLDSSPCAESGDALYYRVVRAHEDAWHILVAKVPKPGADVPHPWGLELQASLSPHFNLQGLCGLVPEGTLPGAPWRGAVALAAEVPERTVAQWLAEACTQPPEEFVWAVALLLLQLSAALKFLEAWGAALVELRPENLLLVAPRGCATTGPPRLLLTDFGRVCLQPPGPPGSPGPHAPQLGSLLRALLSLAAPSTTPLAAGLELLAAQLTRLRPSASRTRGALQALLWGPGPELRGRGAPLGPWLRALGPWLRVRRGLLVLRLAERAAGGEAPSLEDWLCCEYLAEATESSMGQALALLWDLEGGGGADYKDDDDKGPV

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	Homo sapiens

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7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id	8dp5C01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	190 — Delta-Endotoxin; domain 1
Homologous superfamily homologous superfamily	20 — 14-3-3 domain

Domain ID domain_id	8dp5D01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	190 — Delta-Endotoxin; domain 1
Homologous superfamily homologous superfamily	20 — 14-3-3 domain

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8. Citations (1)

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Resolution resolution	3.10 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	169563

fit	/app/data/saxs_computation/dp/8dp5/8dp5.fit
pddf	/app/data/pr_computation/dp/8dp5/8dp5.pr.out
profile	/app/data/saxs_computation/dp/8dp5/8dp5.dat

Structure of the PEAK3/14-3-3 complex

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

Protein PEAK3

State in the Current Structure

Other States of the Same Protein in the Database

14-3-3 protein beta/alpha

State in the Current Structure

Other States of the Same Protein in the Database

14-3-3 protein epsilon

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

Entity 4 Entity 4 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)