Research workbench
Crystal structure of human frizzled 4 cysteine-rich domain (crd)
Analyse Crystal structure of human frizzled 4 cysteine-rich domain (crd) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CM4
- Type
- protein
- Length
- 242 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Frizzled-4
- UniProt
- Q9ULV1
- Ligands
- NAG
- Pockets
- 2 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Frizzled-4 | protein | 121 | 43% helix, 12% strand | Q9ULV1 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 213 | 0.51 | 0.76 | 25 | empty |
| 2 | 108 | 0.41 | 0.77 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 325 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide, 4 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 5CM4 · PDBe 5CM4 · UniProt Q9ULV1
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