Research workbench
Crystal structure of the complete transactivation domain of E2 protein from the human papillomavirus type 16
Analyse Crystal structure of the complete transactivation domain of E2 protein from the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DTO
- Type
- protein
- Length
- 200 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Regulatory protein E2
- UniProt
- P03120
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Regulatory protein E2 | protein | 200 | 39% helix, 26% strand | P03120 |
Compared structures
- 1DTO · Crystal structure of the complete transactivation domain of E2 protein from the human… · 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 P03120
- Elsewhere: RCSB PDB 1DTO · PDBe 1DTO · UniProt P03120
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