Research workbench
Crystal structure of macrocycles containing abeta 15-21 (QKLV(PHI)FA) and abeta 30-36 (AII(SAR)L(ORN)V)
Analyse Crystal structure of macrocycles containing abeta 15-21 (QKLV(PHI)FA) and abeta… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5V64
- Type
- protein
- Length
- 16 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Orn-gln-lys-leu-val-phi-phe-ala-orn-ala-ile-ile-sar-leu- met-val
- Ligands
- NA
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 63% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Orn-gln-lys-leu-val-phi-phe-ala-orn-ala-ile-ile-sar-leu- met-val | protein | 16 | 0% helix, 63% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 4 modified (nonstandard, methylation).
Compared structures
- 5V64 · Crystal structure of macrocycles containing Abeta 15-21 (QKLV(PHI)FA) and Abeta 30-36… · 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 5V64 · PDBe 5V64
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