Research workbench
Wif domain-EGF-like domain 1 of human wnt inhibitory factor 1 in complex with 1,2-dipalmitoylphosphatidylcholine
Analyse Wif domain-EGF-like domain 1 of human wnt inhibitory factor 1 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YGO
- Type
- protein
- Length
- 180 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Wnt inhibitory factor 1
- UniProt
- Q9Y5W5
- Ligands
- PCF, NAG, NA
- Pockets
- 1 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Wnt inhibitory factor 1 | protein | 180 | 9% helix, 39% strand | Q9Y5W5 |
Ligands and binding sites
- PCF · 1,2-diacyl-sn-glycero-3-phoshocholine · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
- NA · Sodium ion · metal · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 508 | 0.82 | 0.88 | 43 | PCF |
Modifications
Observed in the structure: 6 modified, 4 disulfide, 1 glycan (methylation, disulfide, N-glycosylation).
Compared structures
- 2YGO · WIF domain-EGF-like domain 1 of human Wnt inhibitory factor 1 in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9Y5W5 · AlphaFold monomer V2.0 prediction for wnt inhibitory factor 1 (Q9Y5W5) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q9Y5W5
- Elsewhere: RCSB PDB 2YGO · PDBe 2YGO · UniProt Q9Y5W5
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