Research workbench
Structure of the monomeric N-terminal domain of HPV16 E6 oncoprotein
Analyse Structure of the monomeric N-terminal domain of HPV16 E6 oncoprotein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LJX
- Type
- protein
- Length
- 82 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein E6
- UniProt
- P03126
- Ligands
- ZN
Structure
solution nmr · 1 distinct chain · 28% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein E6 | protein | 82 | 28% helix, 12% strand | P03126 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2LJX · Structure of the monomeric N-terminal domain of HPV16 E6 oncoprotein · 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 2LJX · PDBe 2LJX · UniProt P03126
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