Research workbench
Structure of HPV18 E6 oncoprotein in complex with mutant E6AP lxxll motif
Analyse Structure of HPV18 E6 oncoprotein in complex with mutant E6AP lxxll motif in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SJV
- Type
- protein
- Length
- 529 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maltodextrin-binding PROTEIN,PROTEIN E6,UBIQUITIN-protein ligase E3A
- EC
- 2.3.2.26
- UniProt
- A0A376KDN7, P06463, Q05086
- Ligands
- GLC, ZN
- Pockets
- 5 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maltodextrin-binding PROTEIN,PROTEIN E6,UBIQUITIN-protein ligase E3A (EC 2.3.2.26) | protein | 529 | 44% helix, 19% strand | A0A376KDN7, P06463, Q05086 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A
- ZN · Zinc ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 624 | 0.78 | 0.83 | 59 | empty |
| 2 | 290 | 0.71 | 0.84 | 29 | GLC |
| 3 | 177 | 0.51 | 0.77 | 17 | empty |
| 4 | 212 | 0.50 | 0.75 | 30 | empty |
| 5 | 97 | 0.42 | 0.77 | 20 | empty |
Compared structures
- 6SJV · Structure of HPV18 E6 oncoprotein in complex with mutant E6AP LxxLL motif · the same entry in another collection · chain A against A, TM-score 1.00
- Q05086 · AlphaFold monomer V2.0 prediction for ubiquitin-protein ligase E3A (Q05086) · a predicted model of the same protein · chain A against A, TM-score 0.32
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 A0A376KDN7
- Every structure of UniProt P06463
- Every structure of UniProt Q05086
- Elsewhere: RCSB PDB 6SJV · PDBe 6SJV · UniProt A0A376KDN7 · UniProt P06463 · UniProt Q05086
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