Research workbench
E2 DNA-binding domain from papillomavirus bpv-1
Analyse E2 DNA-binding domain from papillomavirus bpv-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DBD
- Type
- protein
- Length
- 200 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Regulatory protein E2
- UniProt
- P03122
- Pockets
- 2 · best druggability 0.67
Structure
solution nmr · 1 distinct chain · 27% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Regulatory protein E2 | protein | 100 | 27% helix, 26% strand | P03122 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 50 | 0.67 | 0.96 | 19 | empty |
| 2 | 57 | 0.49 | 0.86 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1805 Ų buried · 33 hydrogen bonds · protein-protein
Compared structures
- 1DBD · E2 DNA-binding domain from papillomavirus bpv-1 · 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 P03122
- Elsewhere: RCSB PDB 1DBD · PDBe 1DBD · UniProt P03122
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