Research workbench
Bicyclic peptide BP65 crystallized as racemic mixture at 0.9 ångström resolution
Analyse Bicyclic peptide BP65 crystallized as racemic mixture at 0.9 ångström resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6Y14
- Type
- protein
- Length
- 22 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BP65
- Ligands
- O65, NH2
Structure
x-ray diffraction · 1 distinct chain · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | BP65 | protein | 11 | 73% helix, 0% strand | — |
Ligands and binding sites
- O65 · 3,5-bis(hydroxymethyl)-4-methyl-benzaldehyde · ligand · 2 copies · chains A, B
- NH2 · Amino group · ion · 2 copies · chains A, B
- CIT · Citric acid · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 68 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 covalent (covalent ligand).
Compared structures
- 6Y14 · Bicyclic peptide bp65 crystallized as racemic mixture at 0.9 Angstrom resolution · the same entry in another collection · chain B against B, 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 6Y14 · PDBe 6Y14
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