Research workbench
Structure of cyclic D-leu-N-methyl-D-phe-2-abz-D-ala at 0.76 ångström
Analyse Structure of cyclic D-leu-N-methyl-D-phe-2-abz-D-ala at 0.76 ångström 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
- 10 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclic dle-zae-BE2-dal
- Ligands
- BE2, DAL
Structure
x-ray diffraction · 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 | 2 | 0% helix, 0% strand | — |
Ligands and binding sites
- BE2 · 2-aminobenzoic acid · ligand · 5 copies · chains A, C, B, D, E
- DAL · D-alanine · ligand · 5 copies · chains A, C, B, D, E
- EOH · Ethanol · additive · 3 copies · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- C–D · 74 Ų buried · 0 hydrogen bonds · protein-protein
- B–D · 62 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 13 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 covalent, 5 d-amino, 5 modified (covalent ligand, D-amino acid, nonstandard).
Compared structures
- 6ANN · Structure of cyclic D-Leu-N-methyl-D-Phe-2-Abz-D-Ala at 0.76 Angstrom · 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 6ANN · PDBe 6ANN
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