MolNFT v1 · #9458 · protein
Crystal structure of N-terminal domain of drosophila AP180
1HX8 · Synapse-enriched clathrin adaptor protein lap: “Crystal structure of N-terminal domain of drosophila AP180”. X-ray diffraction, 1 ligand (SO4), 4 pockets (best druggability 0.63). MolNFT v1 #9458 on GenesisL1: 3D structure, binding…
- PDB
- 1HX8
- Type
- protein
- Length
- 539 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Synapse-enriched clathrin adaptor protein lap
- UniProt
- Q9VI75
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 68% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Synapse-enriched clathrin adaptor protein lap | protein | 270 | 69% helix, 0% strand | Q9VI75 |
| B | Synapse-enriched clathrin adaptor protein lap | protein | 269 | 68% helix, 0% strand | Q9VI75 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 325 | 0.63 | 0.79 | 31 | empty |
| 2 | 287 | 0.59 | 0.78 | 31 | empty |
| 3 | 121 | 0.54 | 0.82 | 24 | empty |
| 4 | 65 | 0.29 | 0.73 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1135 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 1HX8 · Crystal structure of N-terminal domain of drosophila AP180 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9VI75 · AlphaFold monomer V2.0 prediction for phosphatidylinositol-binding clathrin assembly… · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q9VI75
- Elsewhere: RCSB PDB 1HX8 · PDBe 1HX8 · UniProt Q9VI75
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