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UniProt P37840

Alpha-synuclein (P37840)

Alpha-synuclein (UniProt P37840): 130 experimental structures on GenesisL1, 9 ligands bound, 165 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
P37840
Protein
Alpha-synuclein
Experimental structures
130
Predicted models
0
Ligands
9
Pockets
165 · 27 records with a druggable one

Structures

130 records of P37840 in the MolNFT archive: 130 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
1XQ8Human micelle-bound alpha-synucleinsolution nmrA——
1XQ8Human micelle-bound alpha-synucleinsolution nmrA——
2JN5Solution Structure of a Dodecapeptide from Alpha-Synuclein Bound with Synphilin-1solution nmrA——
2JN5Solution structure of a dodecapeptide from alpha-synuclein bound with synphilin-1solution nmrA——
2KKWSLAS-micelle bound alpha-synucleinsolution nmr, eprA——
2KKWSlas-micelle bound alpha-synucleinsolution nmr; eprA——
2M55NMR structure of the complex of an N-terminally acetylated alpha-synuclein peptide with calmodulinsolution nmrB——
2M55NMR structure of the complex of an N-terminally acetylated alpha- synuclein peptide with calmodulinsolution nmrB——
2N0AAtomic-resolution structure of alpha-synuclein fibrilssolid-state nmrA, B, C, D, E, F, G, H, I, J——
2N0AAtomic-resolution structure of alpha-synuclein fibrilssolid-state nmrA, B, C, D, E, F, G, H, I, J——
2X6MStructure of a single domain camelid antibody fragment in complex with a C-terminal peptide of…x-ray diffractionB——
2X6MStructure of a single domain camelid antibody fragment in complex with a C-terminal peptide of…x-ray diffractionB——
3Q25Crystal structure of human alpha-synuclein (1-19) fused to maltose binding protein (MBP)x-ray diffractionA——
3Q25Crystal structure of human alpha-synuclein (1-19) fused to maltose binding protein (mbp)x-ray diffractionA——
3Q26Cyrstal structure of human alpha-synuclein (10-42) fused to maltose binding protein (MBP)x-ray diffractionA——
3Q26Cyrstal structure of human alpha-synuclein (10-42) fused to maltose binding protein (mbp)x-ray diffractionA——
3Q27Cyrstal structure of human alpha-synuclein (32-57) fused to maltose binding protein (MBP)x-ray diffractionA——
3Q27Cyrstal structure of human alpha-synuclein (32-57) fused to maltose binding protein (mbp)x-ray diffractionA——
3Q28Cyrstal structure of human alpha-synuclein (58-79) fused to maltose binding protein (MBP)x-ray diffractionA——
3Q28Cyrstal structure of human alpha-synuclein (58-79) fused to maltose binding protein (mbp)x-ray diffractionA——
3Q29Cyrstal structure of human alpha-synuclein (1-19) fused to maltose binding protein (MBP)x-ray diffractionA, C——
3Q29Cyrstal structure of human alpha-synuclein (1-19) fused to maltose binding protein (mbp)x-ray diffractionA, C——
4BXLStructure of alpha-synuclein in complex with an engineered binding proteinsolution nmrC——
4BXLStructure of alpha-synuclein in complex with an engineered binding proteinsolution nmrC——
4R0UTgvtava, an amyloid forming segment from alpha synuclein, residues 72-78x-ray diffractionA——
4R0UTgvtava, an amyloid forming segment from alpha synuclein, residues 72- 78x-ray diffractionA——
4R0WVvtgvta, an amyloid forming segment from alpha synuclein, residues 70-76x-ray diffractionA——
4R0WVvtgvta, an amyloid forming segment from alpha synuclein, residues 70- 76x-ray diffractionA——
4RIKAmyloid forming segment, AVVTGVTAV, from the NAC domain of Parkinson's disease protein…x-ray diffractionA——
4RIKAmyloid forming segment, avvtgvtav, from the nac domain of PARKINSON'S disease protein…x-ray diffractionA——
4RILStructure of the amyloid forming segment, GAVVTGVTAVA, from the NAC domain of Parkinson's disease…electron crystallographyA——
4RILStructure of the amyloid forming segment, gavvtgvtava, from the nac domain of PARKINSON'S disease…electron crystallographyA——
4ZNNMicroED structure of the segment, GVVHGVTTVA, from the A53T familial mutant of Parkinson's disease…electron crystallographyA——
4ZNNMicroed structure of the segment, gvvhgvttva, from the A53T familial mutant of PARKINSON'S disease…electron crystallographyA——
6A6BCryo-EM structure of alpha-synuclein fiberelectron microscopyA, B, C, D, E, F, G, H, I, J, K, L——
6CU7Alpha Synuclein fibril formed by full length protein - Rod Polymorphelectron microscopyE, A, B, C, D, F, G, H, I, J——
6CU7Alpha synuclein fibril formed by full length protein - rod polymorphelectron microscopyE, A, B, C, D, F, G, H, I, J——
6CU8Alpha synuclein fibril formed by full length protein - twister polymorphelectron microscopyE, A, B, C, D, F, G, H, I, J——
6FLTStructure of alpha-synuclein fibrilselectron microscopyA, B, C, D, E, F, G, H, I, J——
6H6BStructure of alpha-synuclein fibrilselectron microscopyA, B, C, D, E, F, G, H, I, J——
6H6BStructure of alpha-synuclein fibrilselectron microscopyA, B, C, D, E, F, G, H, I, J——
6I42Structure of the alpha-synuclein PRENAC/CYCLOPHILIN a-complexx-ray diffractionB——
6L1TCryo-EM structure of phosphorylated TYR39 a-synuclein amyloid fibrilelectron microscopyA, B, C, D, E, F, G, H, I, J——
6L1UCryo-EM structure of phosphorylated Tyr39 alpha-synuclein amyloid fibrilelectron microscopyA, B, C, D, E, F, G, H, I, J, K, L, M, N, O——
6L1UCryo-EM structure of phosphorylated TYR39 alpha-synuclein amyloid fibrilelectron microscopyA, B, C, D, E, F, G, H, I, J, K, L, M, N, O——
6L4SCryo-EM structure of alpha-synuclein fiber mutation type E46Kelectron microscopyA, B, C, D, E, F——
6LRQCryo-EM structure of A53T alpha-synuclein amyloid fibrilelectron microscopyA, B, C, D, E, F——
6LRQCryo-EM structure of A53T alpha-synuclein amyloid fibrilelectron microscopyA, B, C, D, E, F——
6OSJCryo-EM structure of the N-terminally acetylated full length alpha-synuclein fibrils (Ac1-140)electron microscopyA, B, C, D, E, F, G, H, I, J—6 (best 0.73)
6OSJCryo-EM structure of the N-terminally acetylated full length alpha- synuclein fibrils (AC1-140)electron microscopyA, B, C, D, E, F, G, H, I, J——
6OSLCryo-EM structure of the N-terminally acetylated C-terminal alpha- synuclein truncation AC1-122electron microscopyA, B, C, D, E, F, G, H, I, J——
6OSMCryo-EM structure of the N-terminally acetylated C-terminal alpha- synuclein truncation AC1-103electron microscopyA, B, C, D, E, F, G, H, I, J——
6PEOCryo-EM structure of alpha-synuclein H50Q narrow fibrilelectron microscopyA, B, C, D, E——
6PESCryo-EM structure of alpha-synuclein H50Q Wide Fibrilelectron microscopyA, B, C, D, E, W, V, X, Y, Z—6 (best 0.70)
6PESCryo-EM structure of alpha-synuclein H50Q wide fibrilelectron microscopyA, B, C, D, E, W, V, X, Y, Z——
6RT0Cryo-EM structure of alpha-synuclein fibril polymorph 2Aelectron microscopyA, B, C, D, E, F, G, H, I, J——
6RTBCryo-EM structure of alpha-synuclein fibril polymorph 2Belectron microscopyH, C, I, D, J, E, G, B, F, A——
6SSTCryo-EM structure of alpha-synuclein fibril polymorph 2Belectron microscopyA, B, C, D, E, F, G, H, I, J——
6SSXCryo-EM structure of alpha-synuclein fibril polymorph 2Aelectron microscopyA, B, C, D, E, F, G, H, I, J——
6UFRStructure of recombinantly assembled E46K alpha-synuclein fibrilselectron microscopyA, C, E, G, I, F, J, D, H, B——

70 records more on the page itself.

Ligands

  • 1KI · 2-bromanyl-4-[(~{E})-2-[6-[2-(2-fluoranylethoxy)ethyl-methyl-amino]-5-methyl-1,3-benzothiazol-2-yl]ethenyl]phenol · in 3 records
  • TFX · 2-[4-(dimethylamino)phenyl]-3,6-dimethyl-1,3-benzothiazol-3-ium · in 3 records
  • COA · Coenzyme A · in 2 records
  • ACE · Acetyl group · in 1 record
  • CMC · Carboxymethyl coenzyme *A · in 1 record
  • IZ8 · 4-azanyl-6-[[4-[4-[(~{E})-(8-azanyl-1-oxidanyl-5,7-disulfo-naphthalen-2-yl)diazenyl]-3-methyl-phenyl]-2-methyl-phenyl]diazenyl]-5-oxidanyl-naphthalene-1,3-disulfonic acid · in 1 record
  • IZV · 2-[4-(methylamino)phenyl]-1,3-benzothiazol-6-ol · in 1 record
  • V79 · copper;trisodium;18-(2-carboxylatoethyl)-20-(carboxylatomethyl)-12-ethenyl-7-ethyl-3,8,13,17-tetramethyl-17,18-dihydroporphyrin-21,23-diide-2-carboxylate · in 1 record
  • Y9W · 2-[(~{E})-4-[6-(methylamino)pyridin-3-yl]but-1-en-3-ynyl]-1,3-benzothiazol-6-ol · in 1 record

Experiment against prediction

Elsewhere

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