MolNFT v1 · #3861 · protein
Structure of E6AP: insights into ubiquitination pathway
1D5F · E6AP hect catalytic domain, E3 ligase: “Structure of E6AP: insights into ubiquitination pathway”. X-ray diffraction, 20 pockets (best druggability 0.83). MolNFT v1 #3861 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1D5F
- Type
- protein
- Length
- 1,050 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E6AP hect catalytic domain, E3 ligase
- EC
- 6.3.2.-
- UniProt
- Q05086
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | E6AP hect catalytic domain, E3 ligase (EC 6.3.2.-) | protein | 350 | 43% helix, 13% strand | Q05086 |
Pockets
20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 675 | 0.83 | 0.87 | 62 | empty |
| 2 | 521 | 0.82 | 0.88 | 57 | empty |
| 3 | 581 | 0.81 | 0.87 | 58 | empty |
| 4 | 504 | 0.80 | 0.87 | 52 | empty |
| 5 | 167 | 0.63 | 0.85 | 24 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1382 Ų buried · 21 hydrogen bonds · protein-protein
- A–C · 1367 Ų buried · 16 hydrogen bonds · protein-protein
- B–C · 1332 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
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 Q05086
- Elsewhere: RCSB PDB 1D5F · PDBe 1D5F · UniProt Q05086
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