Research workbench
Haddock model structure of the N-terminal domain dimer of HPV16 E6
Analyse Haddock model structure of the N-terminal domain dimer of HPV16 E6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LJY
- Type
- protein
- Length
- 140 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein E6
- UniProt
- P03126
- Ligands
- ZN
Structure
solution nmr · 1 distinct chain · 27% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein E6 | protein | 70 | 27% helix, 14% strand | P03126 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 519 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 2LJY · Haddock model structure of the N-terminal domain dimer of HPV16 E6 · the same entry in another collection · chain A against A, 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 P03126
- Elsewhere: RCSB PDB 2LJY · PDBe 2LJY · UniProt P03126
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