MolNFT v1 · #126466 · protein
BEAT FC
5M3V · Ig gamma-1 chain C REGION,IG gamma-3 chain C region: “BEAT FC”. X-ray diffraction, 5 ligands (NAG, MAN, BMA), 4 pockets (best druggability 0.39). MolNFT v1 #126466 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5M3V
- Type
- protein
- Length
- 384 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ig gamma-1 chain C REGION,IG gamma-3 chain C region; Ig gamma-1 chain C region
- UniProt
- P01857, P01860
- Ligands
- NAG, MAN, BMA, GAL, FUL
- Pockets
- 4 · best druggability 0.39
Structure
x-ray diffraction · 2 distinct chains · 11% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ig gamma-1 chain C REGION,IG gamma-3 chain C region | protein | 208 | 10% helix, 48% strand | P01857, P01860 |
| B | Ig gamma-1 chain C region | protein | 176 | 12% helix, 44% strand | P01857 |
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
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 111 | 0.39 | 0.76 | 23 | empty |
| 2 | 86 | 0.37 | 0.77 | 15 | empty |
| 3 | 63 | 0.29 | 0.74 | 18 | empty |
| 4 | 55 | 0.25 | 0.72 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1120 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide, 3 modified, 2 glycan (disulfide, methylation, N-glycosylation, O-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 P01857
- Every structure of UniProt P01860
- Elsewhere: RCSB PDB 5M3V · PDBe 5M3V · UniProt P01857 · UniProt P01860
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.