MolNFT v1 · #137916 · protein
1.80A resolution structure of human IGG3 Fc (N392K)
5W38 · Immunoglobulin heavy constant gamma 3: “1.80A resolution structure of human IGG3 Fc (N392K)”. X-ray diffraction, 2 ligands (NAG, BMA), 1 pocket (best druggability 0.30). MolNFT v1 #137916 on GenesisL1: 3D structure, binding sites…
- PDB
- 5W38
- Type
- protein
- Length
- 418 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Immunoglobulin heavy constant gamma 3
- UniProt
- P01860
- Ligands
- NAG, BMA
- Pockets
- 1 · best druggability 0.30
Structure
x-ray diffraction · 2 distinct chains · 11% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Immunoglobulin heavy constant gamma 3 | protein | 209 | 11% helix, 47% strand | P01860 |
| B | Immunoglobulin heavy constant gamma 3 | protein | 209 | 10% helix, 47% strand | P01860 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B
- BMA · beta-D-mannopyranose · sugar · 2 copies · chains A, B
- FLC · Citrate anion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 64 | 0.30 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1192 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
- 5W38 · 1.80A resolution structure of human IgG3 Fc (N392K) · the same entry in another collection · chain A against A, TM-score 1.00
- P01860 · AlphaFold monomer V2.0 prediction for immunoglobulin heavy constant gamma 3 (P01860) · a predicted model of the same protein · chain B against A, TM-score 0.89
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 P01860
- Elsewhere: RCSB PDB 5W38 · PDBe 5W38 · UniProt P01860
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