MolNFT v1 · #113517 · protein
Cryo-EM structure of helical anth and enth tubules on PI(4,5)P2- containing membranes
5AHV · Enth domain of epsin ENT1: “Cryo-EM structure of helical anth and enth tubules on PI(4,5)P2- containing membranes”. Electron microscopy, 6 pockets (best druggability 0.77). MolNFT v1 #113517 on GenesisL1: 3D structure, binding sites…
- PDB
- 5AHV
- Type
- protein
- Length
- 422 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enth domain of epsin ENT1; Anth domain of endocytic adaptor SLA2
- UniProt
- Q12518, P33338
- Pockets
- 6 · best druggability 0.77
Structure
electron microscopy · 2 distinct chains · 61% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | Enth domain of epsin ENT1 | protein | 154 | 68% helix, 0% strand | Q12518 |
| F | Anth domain of endocytic adaptor SLA2 | protein | 268 | 57% helix, 0% strand | P33338 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 163 | 0.77 | 0.93 | 30 | empty |
| 2 | 692 | 0.73 | 0.79 | 57 | empty |
| 3 | 90 | 0.53 | 0.84 | 20 | empty |
| 4 | 71 | 0.49 | 0.83 | 20 | empty |
| 5 | 68 | 0.39 | 0.79 | 15 | empty |
Interfaces
1 interface between chains.
- E–F · 818 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 5AHV · Cryo-EM structure of helical ANTH and ENTH tubules on PI(4,5)P2-containing membranes · the same entry in another collection · chain E against E, TM-score 1.00
- Q12518 · AlphaFold monomer V2.0 prediction for epsin-1 (Q12518) · a predicted model of the same protein · chain E against A, TM-score 0.86
- P33338 · AlphaFold monomer V2.0 prediction for protein SLA2 (P33338) · a predicted model of the same protein · chain F against A, TM-score 0.74
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 Q12518
- Every structure of UniProt P33338
- Elsewhere: RCSB PDB 5AHV · PDBe 5AHV · UniProt Q12518 · UniProt P33338
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