Research workbench
Designed repeat protein in complex with FZ4
Analyse Designed repeat protein in complex with FZ4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6NE1
- Type
- protein
- Length
- 278 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Frizzled-4; Pfs, nacht and ankyrin domain protein
- UniProt
- Q9ULV1
- Ligands
- NAG
- Pockets
- 1 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Frizzled-4 | protein | 118 | 41% helix, 8% strand | Q9ULV1 |
| B | Pfs, nacht and ankyrin domain protein | protein | 160 | 58% helix, 0% strand | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 80 | 0.46 | 0.81 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1153 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
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 Q9ULV1
- Elsewhere: RCSB PDB 6NE1 · PDBe 6NE1 · UniProt Q9ULV1
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