4rav

Crystal structure of scFvC4 in complex with the first 17 AA of huntingtin

Method: X-RAY DIFFRACTION D_max: 97.3 Å Quality: GOOD

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

Huntingtin

OrganismNot specified

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 E； UniProt 1–17 Chain F； UniProt 1–17	Not recorded	Single-chain Fv, VL × 2 single-chain Fv, VH × 2 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

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 4RAV	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 ligand/ion 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 ligand/ion 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 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 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 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 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 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 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 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 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 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 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 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
6EZ8 Human Huntingtin-HAP40 complex structure Deposited 2017-11-14	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	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 ligand/ion 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 ligand/ion 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 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	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 ligand/ion 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 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 1–38（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 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 1–38（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 ligand/ion 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 ligand/ion 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 ligand/ion 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 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	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 ligand/ion 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 oligomeric state Different ligand/ion 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 ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–3142（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 ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–3142（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	3
Chains and sequence ranges	Author chain E； PDBConstruct 1–17； UniProt 1–17 Author chain F； 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

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	4rav
Deposition date deposition_date	2014-09-11
Structure title title	Crystal structure of scFvC4 in complex with the first 17 AA of huntingtin
Keywords keywords	immunoglobulin fold, immunity, 1-17 residues of huntingtin, IMMUNE SYSTEM-Apoptosis complex; IMMUNE SYSTEM/Apoptosis
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	26.12 Å
Radius of gyration Rg (electron density) rg_electron	25.27 Å
Forward intensity I(0) i0	46291200.00
Molecular weight molecular_weight	50800.0 kDa
Excluded volume excluded_volume	62608 Å³
Envelope volume envelope_volume	77000 Å³
Hydration-shell volume shell_volume	25748 Å³
Envelope diameter envelope_diameter	102.0 Å
Shell Rg shell_rg	31.92 Å
Envelope Rg envelope_rg	25.62 Å
Shape Rg shape_rg	25.20 Å
Total Rg total_rg	26.19 Å
Total atoms total_atoms	3574
Residues n_residues	485
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	97.3 Å
Rg (real space) rg_real	26.17 Å
Rg uncertainty (real space) rg_real_error	0.98 Å
I(0) (real space) i0_real	4.6290e+07
I(0) uncertainty (real space) i0_real_error	7.9690e+05
Rg (reciprocal space) rg_reciprocal	26.16 Å
I(0) (reciprocal space) i0_reciprocal	46290000.0000
Solution quality estimate total_estimate	0.8361
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	30.3 Å
Skewness Skewness skewness	0.420
Kurtosis Kurtosis kurtosis	-0.147
Angular range angular_range	— – 0.3050 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	7104000.0000
Real-space data points n_real_points	62
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.674; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.851; Smooth: 0.992

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	Single-chain Fv, VL
Molecular weight formula_weight	12267.3 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D
Atom count atom_count	3606

SQSALTQPASVSGSPGQSITISCTGTSSDIGAYNYVSWYQQYPGKAPKLLIYDVSNRPSGISNRFSGSKSGDTASLTISGLQAEDEADYYCSSFANSGPLFGGGTKVTVLGHHHHHH

来源 Source

来源生物 organism	Homo sapiens
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	single-chain Fv, VH
Molecular weight formula_weight	13401.8 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

QVQLQESGGGLVQPGGSLRLSCAASGFTFSSYSMSWVRQAPGKGLEWVAVISYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARDRYFDLWGRGTLVTVSSGGGSGGGSGGG

来源 Source

来源生物 organism	Homo sapiens
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 3 Entity 3 polymer

Description description	Huntingtin
Molecular weight formula_weight	1977.4 kDa
Source method src_method	syn
Copy count entity_count	2

Polymer Polymer

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

MATLEKLMKAFESLKSF

Entity 4 Entity 4 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	32

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7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id	4ravA00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	4ravB00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	4ravC00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	4ravD00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

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8. Citations (1)

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Unit-cell length a length_a	151.313 Å
Unit-cell length b length_b	35.933 Å
Unit-cell length c length_c	110.946 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	120.72 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.500 Å
Low-resolution limit resolution_low	44.236 Å
R factor r_factor	0.1820
R_work r_work	0.1796
R_free r_free	0.2263

fit	/app/data/saxs_computation/ra/4rav/4rav.fit
pddf	/app/data/pr_computation/ra/4rav/4rav.pr.out
profile	/app/data/saxs_computation/ra/4rav/4rav.dat

Crystal structure of scFvC4 in complex with the first 17 AA of huntingtin

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

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

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

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (5)

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

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)