MolNFT v1 · #102221 · protein
Crystal structure of mouse NEPH1 D1-D2
4OFD · Kin of irre-like protein 1: “Crystal structure of mouse NEPH1 D1-D2”. X-ray diffraction, 2 ligands (NAG, BMA), 1 pocket (best druggability 0.39). MolNFT v1 #102221 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4OFD
- Type
- protein
- Length
- 387 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kin of irre-like protein 1
- UniProt
- Q80W68
- Ligands
- NAG, BMA
- Pockets
- 1 · best druggability 0.39
Structure
x-ray diffraction · 2 distinct chains · 2% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kin of irre-like protein 1 | protein | 190 | 2% helix, 41% strand | Q80W68 |
| B | Kin of irre-like protein 1 | protein | 197 | 2% helix, 40% strand | Q80W68 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B
- BMA · beta-D-mannopyranose · sugar
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 | 81 | 0.39 | 0.77 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 652 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 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 Q80W68
- Elsewhere: RCSB PDB 4OFD · PDBe 4OFD · UniProt Q80W68
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