MolNFT v1 · #87083 · protein
Crystal structure of the FN5 and FN6 domains of NEO1, form 1
4BQ9 · Neogenin: “Crystal structure of the FN5 and FN6 domains of NEO1, form 1”. X-ray diffraction, 1 ligand (NAG), 2 pockets (best druggability 0.41). MolNFT v1 #87083 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4BQ9
- Type
- protein
- Length
- 392 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Neogenin
- UniProt
- P97798
- Ligands
- NAG
- Pockets
- 2 · best druggability 0.41
Structure
x-ray diffraction · 2 distinct chains · 2% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Neogenin | protein | 205 | 1% helix, 50% strand | P97798 |
| B | Neogenin | protein | 187 | 2% helix, 52% strand | P97798 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 154 | 0.41 | 0.74 | 20 | empty |
| 2 | 96 | 0.35 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 469 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 glycan (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 P97798
- Elsewhere: RCSB PDB 4BQ9 · PDBe 4BQ9 · UniProt P97798
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