MolNFT v1 · #146256 · protein
Rsv-neutralizing human antibody AM22
6DC4 · Fab AM22 heavy chain: “Rsv-neutralizing human antibody AM22”. X-ray diffraction, 4 pockets (best druggability 0.60). MolNFT v1 #146256 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6DC4
- Type
- protein
- Length
- 437 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fab AM22 heavy chain; Fab AM22 light chain
- UniProt
- Q6GMX6, Q8TCD0
- Pockets
- 4 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| H | Fab AM22 heavy chain | protein | 222 | 7% helix, 52% strand | Q6GMX6 |
| L | Fab AM22 light chain | protein | 215 | 7% helix, 53% strand | Q8TCD0 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 17 copies · chains H, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 475 | 0.60 | 0.75 | 49 | EDO |
| 2 | 200 | 0.46 | 0.74 | 32 | EDO |
| 3 | 68 | 0.45 | 0.82 | 23 | EDO |
| 4 | 94 | 0.35 | 0.74 | 17 | empty |
Interfaces
1 interface between chains.
- H–L · 1859 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 6DC4 · RSV-neutralizing human antibody AM22 · the same entry in another collection · chain H against H, 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 Q6GMX6
- Every structure of UniProt Q8TCD0
- Elsewhere: RCSB PDB 6DC4 · PDBe 6DC4 · UniProt Q6GMX6 · UniProt Q8TCD0
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