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UniProt P42858

Huntingtin (P42858)

Huntingtin (UniProt P42858): 45 experimental structures on GenesisL1, 1 ligand bound, 129 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
P42858
Protein
Huntingtin
Experimental structures
45
Predicted models
0
Ligands
1
Pockets
129 · 7 records with a druggable one

Structures

45 records of P42858 in the MolNFT archive: 45 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
2LD0Solution structure of the N-terminal domain of huntingtin (htt17) in 50 % TFEsolution nmrA——
2LD0Solution structure of the N-terminal domain of huntingtin (HTT17) in 50 % tfesolution nmrA——
2LD2Solution structure of the N-terminal domain of huntingtin (htt17) in presence of DPC micellessolution nmrA——
2LD2Solution structure of the N-terminal domain of huntingtin (HTT17) in presence of dpc micellessolution nmrA——
3IO4Huntingtin amino-terminal region with 17 Gln residues - Crystal C90x-ray diffractionA, B, C——
3IO4Huntingtin amino-terminal region with 17 gln residues - crystal C90x-ray diffractionA, B, C——
3IO6Huntingtin amino-terminal region with 17 Gln residues - crystal C92-ax-ray diffractionA, C, B——
3IO6Huntingtin amino-terminal region with 17 gln residues - crystal C92-ax-ray diffractionA, C, B——
3IORHuntingtin amino-terminal region with 17 Gln residues - crystal C95x-ray diffractionA, B, C——
3IORHuntingtin amino-terminal region with 17 gln residues - crystal C95x-ray diffractionA, B, C——
3IOTHuntingtin amino-terminal region with 17 Gln residues - crystal C92-bx-ray diffractionA, B, C——
3IOTHuntingtin amino-terminal region with 17 gln residues - crystal C92-Bx-ray diffractionA, B, C——
3IOUHuntingtin amino-terminal region with 17 Gln residues - crystal C94x-ray diffractionA, B, C——
3IOUHuntingtin amino-terminal region with 17 gln residues - crystal C94x-ray diffractionA, B, C——
3IOVHuntingtin amino-terminal region with 17 Gln residues - crystal C99x-ray diffractionA, B, C——
3IOVHuntingtin amino-terminal region with 17 gln residues - crystal C99x-ray diffractionA, B, C——
3IOWHuntingtin amino-terminal region with 17 Gln residues - crystal C99-Hgx-ray diffractionA, B, C——
3IOWHuntingtin amino-terminal region with 17 gln residues - crystal C99-hgx-ray diffractionA, B, C——
3LRHStructure of anti-huntingtin VL domain in complex with huntingtin peptidex-ray diffractionB, D, F, H, J, L, N, P——
3LRHStructure of anti-huntingtin vl domain in complex with huntingtin peptidex-ray diffractionB, D, F, H, J, L, N, P——
4FE8Crystal Structure of Htt36Q3H-EX1-X1-C1(Alpha)x-ray diffractionA, B, C——
4FE8Crystal structure of HTT36Q3H-EX1-X1-C1(ALPHA)x-ray diffractionA, B, C——
4FEBCrystal Structure of Htt36Q3H-EX1-X1-C2(Beta)x-ray diffractionA, B, C——
4FEBCrystal structure of HTT36Q3H-EX1-X1-C2(BETA)x-ray diffractionA, B, C——
4FECCrystal Structure of Htt36Q3Hx-ray diffractionA, B, C——
4FECCrystal structure of HTT36Q3Hx-ray diffractionA, B, C——
4FEDCrystal Structure of Htt36Q3Hx-ray diffractionA, B, C——
4FEDCrystal structure of HTT36Q3Hx-ray diffractionA, B, C——
4RAVCrystal structure of scFvC4 in complex with the first 17 AA of huntingtinx-ray diffractionE, F——
4RAVCrystal structure of SCFVC4 in complex with the first 17 aa of huntingtinx-ray diffractionE, F——
6EZ8Human huntingtin-HAP40 complex structureelectron microscopyA——
6N8CStructure of the Huntingtin tetramer/dimer mixture determined by paramagnetic NMRsolution nmrA, B, C, D——
6N8CStructure of the huntingtin TETRAMER/DIMER mixture determined by paramagnetic NMRsolution nmrA, B, C, D——
6RMHThe Rigid-body refined model of the normal Huntingtin.electron microscopyA—20 (best 0.82)
6RMHThe rigid-body refined model of the normal huntingtin.electron microscopyA——
6X9OHigh resolution cryoEM structure of huntingtin in complex with HAP40electron microscopyA—19 (best 0.87)
6X9OHigh resolution cryoem structure of huntingtin in complex with HAP40electron microscopyA——
6YEJCryo-EM structure of the Full-length disease type human Huntingtinelectron microscopyA—20 (best 0.80)
6YEJCryo-EM structure of the full-length disease type human huntingtinelectron microscopyA——
7DXJHuman 46QHuntingtin-HAP40 complex structureelectron microscopyA—20 (best 0.90)
7DXJHuman 46QHUNTINGTIN-HAP40 complex structureelectron microscopyA——
7DXKHuman 128QHuntingtin-HAP40 complex structureelectron microscopyA—20 (best 0.89)
7DXKHuman 128QHUNTINGTIN-HAP40 complex structureelectron microscopyA——
8R2OHuntingtin-Q17, 1-66, N-MBP fusionx-ray diffractionA, BGLC10 (best 0.75)
8W15HTT in complex with HAP40 in the apo state.electron microscopyA—20 (best 0.83)

Ligands

  • GLC · alpha-D-glucopyranose · in 1 record

Experiment against prediction

Elsewhere

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