Research workbench
Foldon containing D-amino acids in turn positions
Analyse Foldon containing D-amino acids in turn positions in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WW6
- Type
- protein
- Length
- 81 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fibritin
- UniProt
- Q76VI8
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Fibritin | protein | 27 | 15% helix, 41% strand | Q76VI8 |
Ligands and binding sites
- PG4 · Tetraethylene glycol · additive · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–C · 590 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 584 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 551 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 d-amino (D-amino acid).
Compared structures
- 2WW6 · foldon containing D-amino acids in turn positions · 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
- Every structure of UniProt Q76VI8
- Elsewhere: RCSB PDB 2WW6 · PDBe 2WW6 · UniProt Q76VI8
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