MolNFT v1 · #128507 · protein
Fc dekk heterodimer variant
5NSC: “Fc dekk heterodimer variant”. X-ray diffraction, 5 ligands (NAG, MAN, BMA). MolNFT v1 #128507 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5NSC
- Type
- protein
- Length
- 432 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q6MZV7
- Ligands
- NAG, MAN, BMA, GAL, FUC
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 209 | — | Q6MZV7 |
| B | — | protein | 210 | — | Q6MZV7 |
| C | — | protein | 13 | — | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains A, B
- MAN · alpha-D-mannopyranose · sugar · 4 copies · chains A, B
- BMA · beta-D-mannopyranose · sugar · 2 copies · chains A, B
- GAL · beta-D-galactopyranose · sugar · 2 copies · chains A, B
- FUC · alpha-L-fucopyranose · sugar · 2 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5NSC · Fc DEKK heterodimer variant · the same entry in another collection · chain A against A, TM-score 1.00
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 Q6MZV7
- Elsewhere: RCSB PDB 5NSC · PDBe 5NSC · UniProt Q6MZV7
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