Research workbench
Svqivyk segment from human tau (305-311) displayed on 54-membered macrocycle scaffold (form I)
Analyse Svqivyk segment from human tau (305-311) displayed on 54-membered macrocycle… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4E0M
- Type
- protein
- Length
- 52 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclic pseudo-peptide SVQIVYK(ORN)EF(HAO)(4BF)K(ORN)
- Ligands
- HAO, PO4
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Cyclic pseudo-peptide SVQIVYK(ORN)EF(HAO)(4BF)K(ORN) | protein | 13 | 0% helix, 23% strand | — |
Ligands and binding sites
- HAO · {[3-(hydrazinocarbonyl)-4-methoxyphenyl]amino}(oxo) acetic acid · ligand · 4 copies · chains A, B, C, D
- PO4 · Phosphate ion · ion · 7 copies · chains B, C, D
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 2 copies · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–B · 365 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 355 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 37 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 12 modified, 8 covalent (nonstandard, covalent ligand).
Compared structures
- 4E0M · SVQIVYK segment from human Tau (305-311) displayed on 54-membered macrocycle scaffold… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 4E0M · PDBe 4E0M
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