MolNFT v1 · #15483 · protein
Crystal structure analysis of the immunodominant antigenic site on hepatitis C virus protein bound to mab 19D9D6
1N64 · Fab 19D9D6 light chain: “Crystal structure analysis of the immunodominant antigenic site on hepatitis C virus protein bound to mab…”. X-ray diffraction, 6 pockets (best druggability 0.55). MolNFT v1 #15483 on GenesisL1: 3D…
- PDB
- 1N64
- Type
- protein
- Length
- 454 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fab 19D9D6 light chain; Fab 19D9D6 heavy chain; Genome polyprotein capsid protein C
- EC
- 3.4.22.-, 3.4.21.98, 2.7.7.48
- UniProt
- P29846
- Pockets
- 6 · best druggability 0.55
Structure
x-ray diffraction · 3 distinct chains · 7% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | Fab 19D9D6 light chain | protein | 220 | 6% helix, 52% strand | — |
| H | Fab 19D9D6 heavy chain | protein | 218 | 8% helix, 49% strand | — |
| P | Genome polyprotein capsid protein C (EC 3.4.22.-, 3.4.21.98, 2.7.7.48) | protein | 16 | 19% helix, 0% strand | P29846 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 213 | 0.55 | 0.78 | 31 | empty |
| 2 | 208 | 0.46 | 0.74 | 26 | empty |
| 3 | 84 | 0.35 | 0.76 | 20 | empty |
| 4 | 105 | 0.34 | 0.73 | 21 | empty |
| 5 | 62 | 0.31 | 0.75 | 15 | empty |
Interfaces
3 interfaces between chains.
- L–H · 1799 Ų buried · 14 hydrogen bonds · protein-protein
- H–P · 429 Ų buried · 10 hydrogen bonds · protein-protein
- L–P · 328 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1N64 · Crystal structure analysis of the immunodominant antigenic site on Hepatitis C virus… · the same entry in another collection · chain L against L, 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 P29846
- Elsewhere: RCSB PDB 1N64 · PDBe 1N64 · UniProt P29846
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