MolNFT v1 · #162035 · protein
Protein peptide complex
6QWN: “Protein peptide complex”. X-ray diffraction, 3 ligands (NAG, BMA, MAN). MolNFT v1 #162035 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6QWN
- Type
- protein
- Length
- 1,904 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9LJ64, Q9FZA0
- Ligands
- NAG, BMA, MAN
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 335 | — | Q9LJ64 |
| F, G, H, I, J | — | protein | 47 | — | Q9FZA0 |
| B | — | protein | 338 | — | Q9LJ64 |
| C | — | protein | 338 | — | Q9LJ64 |
| D | — | protein | 336 | — | Q9LJ64 |
| E | — | protein | 322 | — | Q9LJ64 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 13 copies · chains A, B, C, D
- BMA · beta-D-mannopyranose · sugar · 3 copies
- MAN · alpha-D-mannopyranose · sugar
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 Q9LJ64
- Every structure of UniProt Q9FZA0
- Elsewhere: RCSB PDB 6QWN · PDBe 6QWN · UniProt Q9LJ64 · UniProt Q9FZA0
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