Research workbench
Structure of D-leu-D-phe-2-abz-D-ala at 0.64 ångström
Analyse Structure of D-leu-D-phe-2-abz-D-ala at 0.64 ångström in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ANM
- Type
- protein
- Length
- 2 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dle-dpn-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 | Dle-dpn-BE2-dal | protein | 2 | 0% helix, 0% 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: 2 d-amino, 1 covalent (D-amino acid, covalent ligand).
Compared structures
- 6ANM · Structure of D-Leu-D-Phe-2-Abz-D-Ala at 0.64 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 6ANM · PDBe 6ANM
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