7dxj

Human 46QHuntingtin-HAP40 complex structure

Method: ELECTRON MICROSCOPY D_max: 148.3 Å Quality: GOOD

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

Huntingtin

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–38 Chain A； UniProt 39–3142	Not recorded	40-kDa huntingtin-associated protein × 1 （P23610）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7 cryo-EM vitrification conditions：Cryogen ETHANE-PROPANE	Resolution 3.60 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 7DXJ	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2LD0 Solution structure of the N-terminal domain of huntingtin (htt17) in 50 % TFE Deposited 2011-05-13	Different construct Different mutation/modification 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 1–17（17 aa） Fragment：N-terminal residues 1-17	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.2；293 K；Ionic strength (raw mmCIF value) 0.15；Pressure ambient NMR sample composition 0.2 - 0.3 mM 15N labeled at PHE11 htt17, 10 % D2O, 50 % d3 TFE, 40 % PBS, trifluoroethanol/water \| trifluoroethanol/water	Resolution not provided
2LD2 Solution structure of the N-terminal domain of huntingtin (htt17) in presence of DPC micelles Deposited 2011-05-13	Different construct Different mutation/modification 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 1–17（17 aa） Fragment：N-terminal residues 1-17	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；293 K；Ionic strength (raw mmCIF value) 0.025；Pressure ambient NMR sample composition 0.2-0.3 mM 15N labeled at PHE11 htt17, 10 % D2O, 25 mM sodium phosphate, 100 mM d38 DPC, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
3IO4 Huntingtin amino-terminal region with 17 Gln residues - Crystal C90 Deposited 2009-08-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–64（64 aa） Fragment：Fusion protein, see remark 999 Chain B 1–64（64 aa） Fragment：Fusion protein, see remark 999 Chain C 1–64（64 aa） Fragment：Fusion protein, see remark 999	Not recorded	ZN ZINC ION × 8 CA CALCIUM ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.2；277 K；12% polyethylene glycol, 200 mM Zn Acetate, 200 mM Sodium Acetate, 100 mM Sodium Cacodylate pH 6.5 to 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 3.63 Å R-free 0.304
3IO6 Huntingtin amino-terminal region with 17 Gln residues - crystal C92-a Deposited 2009-08-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–64（64 aa） Fragment：FUSION PROTEIN, SEE REMARK 999 Chain B 1–64（64 aa） Fragment：FUSION PROTEIN, SEE REMARK 999 Chain C 1–64（64 aa） Fragment：FUSION PROTEIN, SEE REMARK 999	Not recorded	ZN ZINC ION × 5 CA CALCIUM ION × 9	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.2；pH 7.2, VAPOR DIFFUSION, HANGING DROP	Resolution 3.70 Å R-free 0.293
3IOR Huntingtin amino-terminal region with 17 Gln residues - crystal C95 Deposited 2009-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–64（64 aa） Fragment：Fusion protein, see remark 999 Chain B 1–64（64 aa） Fragment：Fusion protein, see remark 999 Chain C 1–64（64 aa） Fragment：Fusion protein, see remark 999	Not recorded	ZN ZINC ION × 6 CA CALCIUM ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；278 K；12% PEG 4000, 200 mM Zn acetate, 200 mM Sodium acetate, 100 mM Sodium Cacodylate pH 6.5-7.4 , VAPOR DIFFUSION, HANGING DROP, temperature 278K	Resolution 3.60 Å R-free 0.267
3IOT Huntingtin amino-terminal region with 17 Gln residues - crystal C92-b Deposited 2009-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–64（64 aa） Fragment：Fusion protein, see remark 999,Fusion protein, see remark 999 Chain B 1–64（64 aa） Fragment：Fusion protein, see remark 999,Fusion protein, see remark 999 Chain C 1–64（64 aa） Fragment：Fusion protein, see remark 999,Fusion protein, see remark 999	Not recorded	ZN ZINC ION × 9 CA CALCIUM ION × 9	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；278 K；12% PEG 4000, 200 mM Zn acetate, 200 mM Sodium acetate, 100 mM Sodium Cacodylate pH 6.5-7.4, VAPOR DIFFUSION, HANGING DROP, temperature 278K	Resolution 3.50 Å R-free 0.295
3IOU Huntingtin amino-terminal region with 17 Gln residues - crystal C94 Deposited 2009-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–64（64 aa） Fragment：Fusion protein, see remark 999,Fusion protein, see remark 999 Chain B 1–64（64 aa） Fragment：Fusion protein, see remark 999,Fusion protein, see remark 999 Chain C 1–64（64 aa） Fragment：Fusion protein, see remark 999,Fusion protein, see remark 999	Not recorded	ZN ZINC ION × 8 CA CALCIUM ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；278 K；12% PEG 4000, 200 mM Zn acetate, 200 mM Sodium acetate, 100 mM Sodium Cacodylate pH 6.5-7.4, VAPOR DIFFUSION, HANGING DROP, temperature 278K	Resolution 3.70 Å R-free 0.299
3IOV Huntingtin amino-terminal region with 17 Gln residues - crystal C99 Deposited 2009-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–64（64 aa） Fragment：Fusion protein, see remark 999,Fusion protein, see remark 999 Chain B 1–64（64 aa） Fragment：Fusion protein, see remark 999,Fusion protein, see remark 999 Chain C 1–64（64 aa） Fragment：Fusion protein, see remark 999,Fusion protein, see remark 999	Not recorded	ZN ZINC ION × 6 CA CALCIUM ION × 7	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；278 K；12% PEG 4000, 200 mM Zn acetate, 200 mM Sodium acetate, 100 mM Sodium Cacodylate pH 6.5-7.4, VAPOR DIFFUSION, HANGING DROP, temperature 278K	Resolution 3.70 Å R-free 0.280
3IOW Huntingtin amino-terminal region with 17 Gln residues - crystal C99-Hg Deposited 2009-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–64（64 aa） Fragment：Fusion protein, see remark 999,Fusion protein, see remark 999 Chain B 1–64（64 aa） Fragment：Fusion protein, see remark 999,Fusion protein, see remark 999 Chain C 1–64（64 aa） Fragment：Fusion protein, see remark 999,Fusion protein, see remark 999	Not recorded	ZN ZINC ION × 7 CA CALCIUM ION × 10	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；278 K；12% PEG 4000, 200 mM Zn acetate, 200 mM Sodium acetate, 100 mM Sodium Cacodylate pH 6.5-7.4, VAPOR DIFFUSION, HANGING DROP, temperature 278K	Resolution 3.50 Å R-free 0.281
3LRH Structure of anti-huntingtin VL domain in complex with huntingtin peptide Deposited 2010-02-11	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 B 5–18（14 aa） Fragment：huntingtin peptide	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.1；293 K；10 % PEG600, 0.1 mM potassium phosphate dibasic/citric acid, pH 4.1, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.60 Å R-free 0.278
3LRH Structure of anti-huntingtin VL domain in complex with huntingtin peptide Deposited 2010-02-11	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 5–18（14 aa） Fragment：huntingtin peptide	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.1；293 K；10 % PEG600, 0.1 mM potassium phosphate dibasic/citric acid, pH 4.1, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.60 Å R-free 0.278
3LRH Structure of anti-huntingtin VL domain in complex with huntingtin peptide Deposited 2010-02-11	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 5–18（14 aa） Fragment：huntingtin peptide	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.1；293 K；10 % PEG600, 0.1 mM potassium phosphate dibasic/citric acid, pH 4.1, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.60 Å R-free 0.278
3LRH Structure of anti-huntingtin VL domain in complex with huntingtin peptide Deposited 2010-02-11	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 5–18（14 aa） Fragment：huntingtin peptide	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.1；293 K；10 % PEG600, 0.1 mM potassium phosphate dibasic/citric acid, pH 4.1, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.60 Å R-free 0.278
3LRH Structure of anti-huntingtin VL domain in complex with huntingtin peptide Deposited 2010-02-11	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain J 5–18（14 aa） Fragment：huntingtin peptide	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.1；293 K；10 % PEG600, 0.1 mM potassium phosphate dibasic/citric acid, pH 4.1, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.60 Å R-free 0.278
3LRH Structure of anti-huntingtin VL domain in complex with huntingtin peptide Deposited 2010-02-11	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 6 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain L 5–18（14 aa） Fragment：huntingtin peptide	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.1；293 K；10 % PEG600, 0.1 mM potassium phosphate dibasic/citric acid, pH 4.1, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.60 Å R-free 0.278
3LRH Structure of anti-huntingtin VL domain in complex with huntingtin peptide Deposited 2010-02-11	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 7 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain N 5–18（14 aa） Fragment：huntingtin peptide	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.1；293 K；10 % PEG600, 0.1 mM potassium phosphate dibasic/citric acid, pH 4.1, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.60 Å R-free 0.278
3LRH Structure of anti-huntingtin VL domain in complex with huntingtin peptide Deposited 2010-02-11	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 8 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain P 5–18（14 aa） Fragment：huntingtin peptide	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.1；293 K；10 % PEG600, 0.1 mM potassium phosphate dibasic/citric acid, pH 4.1, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.60 Å R-free 0.278
4FE8 Crystal Structure of Htt36Q3H-EX1-X1-C1(Alpha) Deposited 2012-05-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–64（64 aa） Fragment：Huntingtin protein exon1 domain (UNP residues 1-164),Huntingtin protein exon1 domain (UNP residues 1-164) Chain B 1–64（64 aa） Fragment：Huntingtin protein exon1 domain (UNP residues 1-164),Huntingtin protein exon1 domain (UNP residues 1-164) Chain C 1–64（64 aa） Fragment：Huntingtin protein exon1 domain (UNP residues 1-164),Huntingtin protein exon1 domain (UNP residues 1-164)	Mutation：HQHQH,HQHQH Mutation：HQHQH,HQHQH Mutation：HQHQH,HQHQH	ZN ZINC ION × 31	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；278 K；PEG12K, Na Acetate, Zn Acetate, Na Cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 278K	Resolution 3.00 Å R-free 0.275
4FEB Crystal Structure of Htt36Q3H-EX1-X1-C2(Beta) Deposited 2012-05-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–64（64 aa） Chain B 1–64（64 aa） Chain C 1–64（64 aa）	Mutation：HQHQH Mutation：HQHQH Mutation：HQHQH	ZN ZINC ION × 38 NA SODIUM ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions hanging drop；pH 6.5；278 K；PEG12K, Na Acetate, Zn Acetate, Na Cacodylate, pH 6.5, hanging drop, temperature 278K	Resolution 2.80 Å R-free 0.275
4FEC Crystal Structure of Htt36Q3H Deposited 2012-05-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–64（64 aa） Fragment：Huntingtin protein exon1 domain Chain B 1–64（64 aa） Fragment：Huntingtin protein exon1 domain Chain C 1–64（64 aa） Fragment：Huntingtin protein exon1 domain	Mutation：HQHQH,HQHQH Mutation：HQHQH,HQHQH Mutation：HQHQH,HQHQH	ZN ZINC ION × 31	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；278 K；PEG12K, Na Acetate, Zn Acetate, Na Cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 278K	Resolution 3.00 Å R-free 0.275
4FED Crystal Structure of Htt36Q3H Deposited 2012-05-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–64（64 aa） Fragment：Huntingtin protein exon1 domain,Huntingtin protein exon1 domain Chain B 1–64（64 aa） Fragment：Huntingtin protein exon1 domain,Huntingtin protein exon1 domain Chain C 1–64（64 aa） Fragment：Huntingtin protein exon1 domain,Huntingtin protein exon1 domain	Mutation：HQHQH Mutation：HQHQH Mutation：HQHQH	ZN ZINC ION × 35 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；278 K；PEG12K, Na Acetate, Zn Acetate, Na Cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 278K	Resolution 2.81 Å R-free 0.269
4RAV Crystal structure of scFvC4 in complex with the first 17 AA of huntingtin Deposited 2014-09-11	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain E 1–17（17 aa） Chain F 1–17（17 aa）	Not recorded	SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.6；291 K；0.2 M ammonium sulphate, 25% PEG 4000 and 0.1 M sodium acetate buffer at pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 291K	Resolution 2.50 Å R-free 0.226
6EZ8 Human Huntingtin-HAP40 complex structure Deposited 2017-11-14	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–3142（3142 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 4.00 Å
6N8C Structure of the Huntingtin tetramer/dimer mixture determined by paramagnetic NMR Deposited 2018-11-29	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–24（23 aa） Chain B 2–24（23 aa） Chain C 2–24（23 aa） Chain D 2–24（23 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；278 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR measurement conditions pH 6.5；283 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR sample composition 1 mM [U-13C; U-15N] httNT-Q7, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1 mM 2-13C glucose; U-15N httNT-Q7, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.6 mM [U-15N] httNT-Q7, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.75 mM 2-13C glucose; U-15N httNT-Q7, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.4 mM 2-13C glucose; U-15N httNT-Q7, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
6RMH The Rigid-body refined model of the normal Huntingtin. Deposited 2019-05-06	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–3142（3142 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE；blot 9 seconds incubate 30 seconds	Resolution 9.60 Å
6X9O High resolution cryoEM structure of huntingtin in complex with HAP40 Deposited 2020-06-03	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–3142（3142 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.60 Å
6YEJ Cryo-EM structure of the Full-length disease type human Huntingtin Deposited 2020-03-24	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 18–3142（3125 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE；30 seconds incubation 8 seconds blotting	Resolution 18.20 Å
7DXK Human 128QHuntingtin-HAP40 complex structure Deposited 2021-01-19	Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–38（38 aa） Chain A 39–3142（3104 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 4.10 Å
8R2O Huntingtin-Q17, 1-66, N-MBP fusion Deposited 2023-11-07	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–64（64 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.25；293 K；0.8 M KH2PO4, 0.8 M NaH2PO4, and 0.1 M TRIS/HCl pH 8.25	Resolution 3.23 Å R-free 0.238
8R2O Huntingtin-Q17, 1-66, N-MBP fusion Deposited 2023-11-07	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1–64（64 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.25；293 K；0.8 M KH2PO4, 0.8 M NaH2PO4, and 0.1 M TRIS/HCl pH 8.25	Resolution 3.23 Å R-free 0.238
8SAH Huntingtin C-HEAT domain in complex with HAP40 Deposited 2023-03-31	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 2093–3136（1044 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
8VLX HTT in complex with HAP40 and a small molecule. Deposited 2024-01-12	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–3142（3142 aa）	Not recorded	A1ACS N-[(1S,2R)-2-benzylcyclopentyl]-N'-{1-[(1S)-1-(pyridin-4-yl)ethyl]piperidin-4-yl}urea × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；25 mM Hepes, 300 mM NaCl, 0.025%CHAPS, 1mM DTT, 1mM Ligand, 1% DMSO cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.60 Å
8W15 HTT in complex with HAP40 in the apo state. Deposited 2024-02-15	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–3142（3142 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；25 mM Hepes, 300 mM NaCl, 0.025%CHAPS, 1mM DTT, 1% DMSO cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.72 Å
8YAE Cryo-ET structure of huntingtin actin complex Deposited 2024-02-09	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: tetradecameric	Chain A 1–3142（3142 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 10.08 Å
8YAO Cryo-ET structure of huntingtin actin dimer complex Deposited 2024-02-09	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 28 PDB declaration: 28-meric	Chain A 1–3142（3142 aa） Chain a 1–3142（3142 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 20.80 Å
9PMW Structure of HTTQ23-HAP40 complex bound to macrocycles HHL1, HD4 and HL2 Deposited 2025-07-18	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–3142（3142 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.10 Å
9PN0 Structure of HTTQ23-HAP40 complex bound to macrocycles HHD3, HD4 and HL2 Deposited 2025-07-18	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–3142（3142 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.30 Å
9YR6 Structure of HTTQ23-HAP40 complex bound to a small molecule ligand Deposited 2025-10-16	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–3142（3142 aa）	Not recorded	A1CYY 2-[(1R)-2,2-difluorocyclopropyl]-N-[(1-methyl-1H-indazol-6-yl)methyl]aniline × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.30 Å

30 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	HD_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–38； UniProt 1–38 Author chain A； PDBConstruct 64–3167； UniProt 39–3142

40-kDa huntingtin-associated protein

Homo sapiens

UniProt P23610

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 B； UniProt 1–371	Not recorded	Huntingtin × 1 （P42858）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7 cryo-EM vitrification conditions：Cryogen ETHANE-PROPANE	Resolution 3.60 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 7DXJ	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6EZ8 Human Huntingtin-HAP40 complex structure Deposited 2017-11-14	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–371（371 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 4.00 Å
6X9O High resolution cryoEM structure of huntingtin in complex with HAP40 Deposited 2020-06-03	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–371（371 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.60 Å
7DXK Human 128QHuntingtin-HAP40 complex structure Deposited 2021-01-19	Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–371（371 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 4.10 Å
8SAH Huntingtin C-HEAT domain in complex with HAP40 Deposited 2023-03-31	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–371（371 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
8VLX HTT in complex with HAP40 and a small molecule. Deposited 2024-01-12	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–371（371 aa）	Not recorded	A1ACS N-[(1S,2R)-2-benzylcyclopentyl]-N'-{1-[(1S)-1-(pyridin-4-yl)ethyl]piperidin-4-yl}urea × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；25 mM Hepes, 300 mM NaCl, 0.025%CHAPS, 1mM DTT, 1mM Ligand, 1% DMSO cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.60 Å
8W15 HTT in complex with HAP40 in the apo state. Deposited 2024-02-15	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–371（371 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；25 mM Hepes, 300 mM NaCl, 0.025%CHAPS, 1mM DTT, 1% DMSO cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.72 Å
9PMW Structure of HTTQ23-HAP40 complex bound to macrocycles HHL1, HD4 and HL2 Deposited 2025-07-18	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 1–371（371 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.10 Å
9PN0 Structure of HTTQ23-HAP40 complex bound to macrocycles HHD3, HD4 and HL2 Deposited 2025-07-18	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 1–371（371 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.30 Å
9YR6 Structure of HTTQ23-HAP40 complex bound to a small molecule ligand Deposited 2025-10-16	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–371（371 aa）	Not recorded	A1CYY 2-[(1R)-2,2-difluorocyclopropyl]-N-[(1-methyl-1H-indazol-6-yl)methyl]aniline × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.30 Å

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

View Construct and Data Evidence

UniProt name	HAP40_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–371； UniProt 1–371

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	7dxj
Deposition date deposition_date	2021-01-19
Structure title title	Human 46QHuntingtin-HAP40 complex structure
Keywords keywords	Huntingtin, 46Q, HAP40, STRUCTURAL PROTEIN; STRUCTURAL 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	46.40 Å
Radius of gyration Rg (electron density) rg_electron	45.88 Å
Forward intensity I(0) i0	1153710000.00
Molecular weight molecular_weight	291700.0 kDa
Excluded volume excluded_volume	369560 Å³
Envelope volume envelope_volume	519620 Å³
Hydration-shell volume shell_volume	91123 Å³
Envelope diameter envelope_diameter	148.7 Å
Shell Rg shell_rg	53.25 Å
Envelope Rg envelope_rg	45.09 Å
Shape Rg shape_rg	45.89 Å
Total Rg total_rg	46.15 Å
Total atoms total_atoms	20491
Residues n_residues	2621
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	148.3 Å
Rg (real space) rg_real	46.20 Å
Rg uncertainty (real space) rg_real_error	0.90 Å
I(0) (real space) i0_real	1.1540e+09
I(0) uncertainty (real space) i0_real_error	1.9370e+07
Rg (reciprocal space) rg_reciprocal	46.39 Å
I(0) (reciprocal space) i0_reciprocal	1154000000.0000
Solution quality estimate total_estimate	0.8936
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	56.7 Å
Skewness Skewness skewness	0.192
Kurtosis Kurtosis kurtosis	-0.529
Angular range angular_range	— – 0.1700 Å⁻¹
Current regularization parameter α current_alpha	0.0001
Highest regularization parameter α highest_alpha	142900000.0000
Real-space data points n_real_points	35
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.911; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.898

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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	Huntingtin
Molecular weight formula_weight	351191.3 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	20491

MATLEKLMKAFESLKSFQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQPPPPPPPPPPPQLPQPPPQAQPLLPQPQPPPPPPPPPPGPAVAEEPLHRPKKELSATKKDRVNHCLTICENIVAQSVRNSPEFQKLLGIAMELFLLCSDDAESDVRMVADECLNKVIKALMDSNLPRLQLELYKEIKKNGAPRSLRAALWRFAELAHLVRPQKCRPYLVNLLPCLTRTSKRPEESVQETLAAAVPKIMASFGNFANDNEIKVLLKAFIANLKSSSPTIRRTAAGSAVSICQHSRRTQYFYSWLLNVLLGLLVPVEDEHSTLLILGVLLTLRYLVPLLQQQVKDTSLKGSFGVTRKEMEVSPSAEQLVQVYELTLHHTQHQDHNVVTGALELLQQLFRTPPPELLQTLTAVGGIGQLTAAKEESGGRSRSGSIVELIAGGGSSCSPVLSRKQKGKVLLGEEEALEDDSESRSDVSSSALTASVKDEISGELAASSGVSTPGSAGHDIITEQPRSQHTLQADSVDLASCDLTSSATDGDEEDILSHSSSQVSAVPSDPAMDLNDGTQASSPISDSSQTTTEGPDSAVTPSDSSEIVLDGTDNQYLGLQIGQPQDEDEEATGILPDEASEAFRNSSMALQQAHLLKNMSHCRQPSDSSVDKFVLRDEATEPGDQENKPCRIKGDIGQSTDDDSAPLVHCVRLLSASFLLTGGKNVLVPDRDVRVSVKALALSCVGAAVALHPESFFSKLYKVPLDTTEYPEEQYVSDILNYIDHGDPQVRGATAILCGTLICSILSRSRFHVGDWMGTIRTLTGNTFSLADCIPLLRKTLKDESSVTCKLACTAVRNCVMSLCSSSYSELGLQLIIDVLTLRNSSYWLVRTELLETLAEIDFRLVSFLEAKAENLHRGAHHYTGLLKLQERVLNNVVIHLLGDEDPRVRHVAAASLIRLVPKLFYKCDQGQADPVVAVARDQSSVYLKLLMHETQPPSHFSVSTITRIYRGYNLLPSITDVTMENNLSRVIAAVSHELITSTTRALTFGCCEALCLLSTAFPVCIWSLGWHCGVPPLSASDESRKSCTVGMATMILTLLSSAWFPLDLSAHQDALILAGNLLAASAPKSLRSSWASEEEANPAATKQEEVWPALGDRALVPMVEQLFSHLLKVINICAHVLDDVAPGPAIKAALPSLTNPPSLSPIRRKGKEKEPGEQASVPLSPKKGSEASAASRQSDTSGPVTTSKSSSLGSFYHLPSYLRLHDVLKATHANYKVTLDLQNSTEKFGGFLRSALDVLSQILELATLQDIGKCVEEILGYLKSCFSREPMMATVCVQQLLKTLFGTNLASQFDGLSSNPSKSQGRAQRLGSSSVRPGLYHYCFMAPYTHFTQALADASLRNMVQAEQENDTSGWFDVLQKVSTQLKTNLTSVTKNRADKNAIHNHIRLFEPLVIKALKQYTTTTCVQLQKQVLDLLAQLVQLRVNYCLLDSDQVFIGFVLKQFEYIEVGQFRESEAIIPNIFFFLVLLSYERYHSKQIIGIPKIIQLCDGIMASGRKAVTHAIPALQPIVHDLFVLRGTNKADAGKELETQKEVVVSMLLRLIQYHQVLEMFILVLQQCHKENEDKWKRLSRQIADIILPMLAKQQMHIDSHEALGVLNTLFEILAPSSLRPVDMLLRSMFVTPNTMASVSTVQLWISGILAILRVLISQSTEDIVLSRIQELSFSPYLISCTVINRLRDGDSNSTLEEHSEGKQIKNLPEETFSRFLLQLVGILLEDIVTKQLKVEMSEQQHTFYCQELGTLLMCLIHIFKSGMFRRITAAATRLFRSDGCGGSFYTLDSLNLRARSMITTHPALVLLWCQILLLVNHTDYRWWAEVQQTPKRHSLSSTKLLSPQMSGEEEDSDLAAKLGMCNREIVRRGALILFCDYVCQNLHDSEHLTWLIVNHIQDLISLSHEPPVQDFISAVHRNSAASGLFIQAIQSRCENLSTPTMLKKTLQCLEGIHLSQSGAVLTLYVDRLLCTPFRVLARMVDILACRRVEMLLAANLQSSMAQLPMEELNRIQEYLQSSGLAQRHQRLYSLLDRFRLSTMQDSLSPSPPVSSHPLDGDGHVSLETVSPDKDWYVHLVKSQCWTRSDSALLEGAELVNRIPAEDMNAFMMNSEFNLSLLAPCLSLGMSEISGGQKSALFEAAREVTLARVSGTVQQLPAVHHVFQPELPAEPAAYWSKLNDLFGDAALYQSLPTLARALAQYLVVVSKLPSHLHLPPEKEKDIVKFVVATLEALSWHLIHEQIPLSLDLQAGLDCCCLALQLPGLWSVVSSTEFVTHACSLIHCVHFILEAVAVQPGEQLLSPERRTNTPKAISEEEEEVDPNTQNPKYITAACEMVAEMVESLQSVLALGHKRNSGVPAFLTPLLRNIIISLARLPLVNSYTRVPPLVWKLGWSPKPGGDFGTAFPEIPVEFLQEKEVFKEFIYRINTLGWTSRTQFEETWATLLGVLVTQPLVMEQEESPPEEDTERTQINVLAVQAITSLVLSAMTVPVAGNPAVSCLEQQPRNKPLKALDTRFGRKLSIIRGIVEQEIQAMVSKRENIATHHLYQAWDPVPSLSPATTGALISHEKLLLQINPERELGSMSYKLGQVSIHSVWLGNSITPLREEEWDEEEEEEADAPAPSSPPTSPVNSRKHRAGVDIHSCSQFLLELYSRWILPSSSARRTPAILISEVVRSLLVVSDLFTERNQFELMYVTLTELRRVHPSEDEILAQYLVPATCKAAAVLGMDKAVAEPVSRLLESTLRSSHLPSRVGALHGVLYVLECDLLDDTAKQLIPVISDYLLSNLKGIAHCVNIHSQQHVLVMCATAFYLIENYPLDVGPEFSASIIQMCGVMLSGSEESTPSIIYHCALRGLERLLLSEQLSRLDAESLVKLSVDRVNVHSPHRAMAALGLMLTCMYTGKEKVSPGRTSDPNPAAPDSESVIVAMERVSVLFDRIRKGFPCEARVVARILPQFLDDFFPPQDIMNKVIGEFLSNQQPYPQFMATVVYKVFQTLHSTGQSSMVRDWVMLSLSNFTQRAPVAMATWSLSCFFVSASTSPWVAAILPHVISRMGKLEQVDVNLFCLVATDFYRHQIEEELDRRAFQSVLEVVAAPGSPYHRLLTCLRNVHKVTTC

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 K-12

Entity 2 Entity 2 polymer

Description description	40-kDa huntingtin-associated protein
Molecular weight formula_weight	39141.9 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

MAAAAAGLGGGGAGPGPEAGDFLARYRLVSNKLKKRFLRKPNVAEAGEQFGQLGRELRAQECLPYAAWCQLAVARCQQALFHGPGEALALTEAARLFLRQERDARQRLVCPAAYGEPLQAAASALGAAVRLHLELGQPAAAAALCLELAAALRDLGQPAAAAGHFQRAAQLQLPQLPLAALQALGEAASCQLLARDYTGALAVFTRMQRLAREHGSHPVQSLPPPPPPAPQPGPGATPALPAALLPPNSGSAAPSPAALGAFSDVLVRCEVSRVLLLLLLQPPPAKLLPEHAQTLEKYSWEAFDSHGQESSGQLPEELFLLLQSLVMATHEKDTEAIKSLQVEMWPLLTAEQNHLLHLVLQETISPSGQGV

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 K-12

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8. Citations (1)

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Resolution resolution	3.60 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	192473

fit	/app/data/saxs_computation/dx/7dxj/7dxj.fit
pddf	/app/data/pr_computation/dx/7dxj/7dxj.pr.out
profile	/app/data/saxs_computation/dx/7dxj/7dxj.dat

Human 46QHuntingtin-HAP40 complex structure

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

Huntingtin

State in the Current Structure

Other States of the Same Protein in the Database

40-kDa huntingtin-associated protein

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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)