Research workbench
Structure of cyclic D-Leu-N-methyl-D-Phe-2-Abz-D-Ala at 0.76 Angstrom
Analyse Structure of cyclic D-Leu-N-methyl-D-Phe-2-Abz-D-Ala at 0.76 Angstrom in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ANN
- Type
- protein
- Length
- 20 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 0.76
- Molecule
- cyclic DLE-ZAE-BE2-DAL
Structure
x-ray diffraction · resolution 0.76 · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | cyclic DLE-ZAE-BE2-DAL | protein | 4 | 0% helix, 0% strand | — |
Ligands and binding sites
- EOH · Ethanol · additive · 3 copies · chains A, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
7 interfaces between chains.
- B–C · 135 Ų buried · 4 hydrogen bonds · protein-protein
- D–E · 133 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 131 Ų buried · 2 hydrogen bonds · protein-protein
- C–D · 100 Ų buried · 0 hydrogen bonds · protein-protein
- B–D · 77 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 d-amino, 10 modified (D-amino acid, nonstandard).
Compared structures
- 6ANN · Structure of cyclic D-leu-N-methyl-D-phe-2-abz-D-ala at 0.76 ångström · the same entry in another collection · chain A against A, TM-score 0.75
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 6ANN · PDBe 6ANN
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