MolNFT v1 · #100555 · protein
Structure of the hepatitis C envelope glycoprotein E1 antigenic region 314-324 bound to the cross-neutralizing antibody IGH526
4N0Y · IGH526 heavy chain: “Structure of the hepatitis C envelope glycoprotein E1 antigenic region 314-324 bound to the…”. X-ray diffraction, 2 ligands (NH2, CL), 4 pockets (best druggability 0.38). MolNFT v1 #100555 on GenesisL1: 3D…
- PDB
- 4N0Y
- Type
- protein
- Length
- 445 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- IGH526 heavy chain; IGH526 light chain; HCV E1 peptide
- UniProt
- R9TE34
- Ligands
- NH2, CL
- Pockets
- 4 · best druggability 0.38
Structure
x-ray diffraction · 3 distinct chains · 9% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| H | IGH526 heavy chain | protein | 222 | 7% helix, 52% strand | — |
| L | IGH526 light chain | protein | 212 | 9% helix, 51% strand | — |
| A | HCV E1 peptide | protein | 11 | 73% helix, 0% strand | R9TE34 |
Ligands and binding sites
- NH2 · Amino group · ion · chains A
- CL · Chloride ion · ion · chains H, L, A
- GOL · Glycerol · additive · 7 copies · chains H, A, 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 71 | 0.38 | 0.78 | 15 | GOL |
| 2 | 95 | 0.38 | 0.76 | 27 | empty |
| 3 | 61 | 0.32 | 0.76 | 17 | empty |
| 4 | 50 | 0.24 | 0.72 | 18 | empty |
Interfaces
3 interfaces between chains.
- H–L · 1719 Ų buried · 11 hydrogen bonds · protein-protein
- H–A · 503 Ų buried · 1 hydrogen bond · protein-protein
- L–A · 213 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 4N0Y · Structure of the Hepatitis C Envelope Glycoprotein E1 antigenic region 314-324 bound to… · 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 R9TE34
- Elsewhere: RCSB PDB 4N0Y · PDBe 4N0Y · UniProt R9TE34
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