2MUS: HADDOCK calculated model of LIN5001
HADDOCK calculated model of LIN5001 bound to the HET-s amyloid. Determined by solution NMR. Released 1 Feb 2017.
- Method
- Solution NMR
- Organism
- Podospora anserina
- Chains
- 5
- Atoms
- 2,804
- Mol. weight
- 43.96 kDa
- Ligands
- 3LS
- Released
- 1 Feb 2017
Explore 2MUS in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
2MUS contains 1 α-helix and 29 β-strands across 5 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
Chain A: 0 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 226-234 | 9 | 1 |
| β-strand | 238-245 | 8 | 2 |
| β-strand | 248 | 1 | 3 |
| β-strand | 250 | 1 | 3 |
| β-strand | 262-270 | 9 | 1 |
| β-strand | 274-281 | 8 | 2 |
Chain B: 1 helix, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 226-227 | 2 | 1 |
| β-strand | 230-234 | 5 | 1 |
| β-strand | 238-241 | 4 | 2 |
| β-strand | 244-245 | 2 | 2 |
| α-helix | 247-249 | 3 | |
| β-strand | 262-270 | 9 | 1 |
| β-strand | 274-277 | 4 | 2 |
| β-strand | 280-281 | 2 | 2 |
| β-strand | 283 | 1 | 4 |
| β-strand | 285 | 1 | 4 |
Chain C: 0 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 226-234 | 9 | 1 |
| β-strand | 238-241 | 4 | 2 |
| β-strand | 244-245 | 2 | 2 |
| β-strand | 262-270 | 9 | 1 |
| β-strand | 274-277 | 4 | 2 |
| β-strand | 280-282 | 3 | 2 |
Chain D: 0 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 226-234 | 9 | 1 |
| β-strand | 238-246 | 9 | 2 |
| β-strand | 262-270 | 9 | 1 |
| β-strand | 273-281 | 9 | 2 |
Chain E: 0 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 226-234 | 9 | 1 |
| β-strand | 237-245 | 9 | 2 |
| β-strand | 262-270 | 9 | 1 |
| β-strand | 274-279 | 6 | 2 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Heterokaryon incompatibility protein s | A, B, C, D, E | protein | 79 | Podospora anserina | Q03689 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E), FASTA
>2MUS_1 Heterokaryon incompatibility protein s (chains A, B, C, D, E)
MKIDAIVGRNSAKDIRTEERARVQLGNVVTAAALHGGIRISDQTTNSVKTVVGKGESRVL
IGNEYGGKGFWDNHHHHHH
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| 3LS | 3''',4'-bis(carboxymethyl)-2,2':5',2'':5'',2''':5''',2''''-quinquethiophene-5,5… | C26 H16 O8 S5 | 1 |
Primary citation
Structure-based drug design identifies polythiophenes as antiprion compounds. Herrmann, U.S., Schutz, A.K., Shirani, H. et al. Sci Transl Med (2015) 7:299ra123-299ra123. DOI 10.1126/scitranslmed.aab1923 · PubMed
Other PDB entries of the same protein (UniProt Q03689 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 2WVQ 2.0 Å, Structure of the HET-s N-terminal domain. Mutant D23A, P33H
- 2WVN 2.62 Å, Structure of the HET-s N-terminal domain
- 2KJ3 High-resolution structure of the HET-s(218-289) prion in its amyloid form obtained by…
- 2LBU HADDOCK calculated model of Congo red bound to the HET-s amyloid
- 2RNM Structure of The HET-s(218-289) prion in its amyloid form obtained by solid-state NMR
Browse structure collections
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