Research workbench
Structure of the epstein-barr virus zebra protein at approximately 3.5 ångström resolution
Analyse Structure of the epstein-barr virus zebra protein at approximately 3.5 ångström… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2C9N
- Type
- protein + DNA
- Length
- 140 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P03206
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | dna | 11 | — | — |
| B | — | dna | 11 | — | — |
| Y, Z | — | protein | 59 | — | P03206 |
Compared structures
- 2C9N · Structure of the Epstein-Barr virus ZEBRA protein at approximately 3. 5 Angstrom… · 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 P03206
- Elsewhere: RCSB PDB 2C9N · PDBe 2C9N · UniProt P03206
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.