MolNFT v1 · #166451 · protein
Mouse IGG2A bispecific Fc
6UQC: “Mouse IGG2A bispecific Fc”. X-ray diffraction, 4 ligands (NAG, MAN, BMA). MolNFT v1 #166451 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6UQC
- Type
- protein
- Length
- 828 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P01865
- Ligands
- NAG, MAN, BMA, FUC
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, D | — | protein | 207 | — | P01865 |
| E, F | — | protein | 207 | — | P01865 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 16 copies · chains C, D, E, F
- MAN · alpha-D-mannopyranose · sugar · 8 copies · chains C, D, E, F
- BMA · beta-D-mannopyranose · sugar · 4 copies · chains C, D, E, F
- FUC · alpha-L-fucopyranose · sugar · 4 copies · chains C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- P01865 · AlphaFold monomer V2.0 prediction for ig gamma-2A chain C region, membrane-bound form… · a predicted model of the same protein · chain E against A, TM-score 0.96
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 P01865
- Elsewhere: RCSB PDB 6UQC · PDBe 6UQC · UniProt P01865
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