MolNFT v2 · #150406 · protein
BEAT Fc with improved heterodimerization (Q3A-D84.4Q)
6G1E: “BEAT Fc with improved heterodimerization (Q3A-D84.4Q)”. X-ray diffraction at 1.88, 5 ligands (NAG, MAN, BMA). MolNFT v2 #150406 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6G1E
- Type
- protein
- Length
- 415 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.88
- Source
- Homo sapiens
- UniProt
- P01857, P01860, P0DOX5
- Ligands
- NAG, MAN, BMA, GAL, FUL
Structure
x-ray diffraction · resolution 1.88 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 208 | — | P01857, P01860 |
| B | — | protein | 207 | — | P0DOX5 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 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
- FUL · beta-L-fucopyranose · sugar · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6G1E · Beat Fc with improved heterodimerization (Q3A-D84.4Q) · 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 P01857
- Every structure of UniProt P01860
- Every structure of UniProt P0DOX5
- Elsewhere: RCSB PDB 6G1E · PDBe 6G1E · UniProt P01857 · UniProt P01860 · UniProt P0DOX5
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