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2ld2

Solution structure of the N-terminal domain of huntingtin (htt17) in presence of DPC micelles

Method: SOLUTION NMR Dmax: 33.8 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Huntingtin

OrganismNot specified

UniProt P42858

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1–17 Fragment：N-terminal residues 1-17 Non-standard monomer：Yes (specific site not provided by mmCIF) No other associated polymer 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

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 2LD2 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 experimental conditions 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
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 oligomeric state 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 oligomeric state 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 oligomeric state 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 oligomeric state 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 oligomeric state 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 oligomeric state 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 oligomeric state 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 oligomeric state 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 mutation/modification 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 oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–3142（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 conditions 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 experimental method 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 oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–3142（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 experimental method 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
7DXJ Human 46QHuntingtin-HAP40 complex structure Deposited 2021-01-19 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 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 3.60 Å
7DXK Human 128QHuntingtin-HAP40 complex structure Deposited 2021-01-19 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 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 oligomeric state Different experimental method 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 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 1–3142（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 oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–3142（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 method 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 mutation/modification Different oligomeric state Different experimental method 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 method 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 method 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 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 1–3142（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 1–17； UniProt 1–17

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 2ld2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2ld2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2ld2
Deposition date deposition_date2011-05-13
Structure title titleSolution structure of the N-terminal domain of huntingtin (htt17) in presence of DPC micelles
Keywords keywordsalpha helix, LIPID BINDING PROTEIN; LIPID BINDING PROTEIN
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier8.12 Å
Radius of gyration Rg (electron density) rg_electron8.56 Å
Forward intensity I(0) i018430600.00
Molecular weight molecular_weight39489.0 kDa
Excluded volume excluded_volume51274 ų
Envelope volume envelope_volume6947 ų
Hydration-shell volume shell_volume6080 ų
Envelope diameter envelope_diameter36.1 Å
Shell Rg shell_rg15.35 Å
Envelope Rg envelope_rg11.49 Å
Shape Rg shape_rg8.45 Å
Total Rg total_rg9.42 Å
Total atoms total_atoms5760
Residues n_residues340
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax33.8 Å
Rg (real space) rg_real8.40 Å
Rg uncertainty (real space) rg_real_error0.53 Å
I(0) (real space) i0_real1.8430e+07
I(0) uncertainty (real space) i0_real_error2.0870e+05
Rg (reciprocal space) rg_reciprocal8.39 Å
I(0) (reciprocal space) i0_reciprocal18430000.0000
Solution quality estimate total_estimate0.6313
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary5.6 Å
Skewness Skewness skewness0.703
Kurtosis Kurtosis kurtosis-0.187
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1025.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.098; Stabil: 0.987; Sysdev: 1.000; Positv: 1.000; Valcen: 0.001; Smooth: 0.946
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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9. Files and Curves (10)