MolNFT v1 · #125973 · protein
Crystal structure of the zebra fish enth domain from EPSIN1 in 1.41 ångström resolution
5LP0 · Epsin 1: “Crystal structure of the zebra fish enth domain from EPSIN1 in 1.41 ångström resolution”. X-ray diffraction, 1 ligand (PO4), 4 pockets (best druggability 0.74). MolNFT v1 #125973 on GenesisL1: 3D structure, binding sites…
- PDB
- 5LP0
- Type
- protein
- Length
- 548 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Epsin 1
- UniProt
- F1Q523
- Ligands
- PO4
- Pockets
- 4 · best druggability 0.74
Structure
x-ray diffraction · 4 distinct chains · 74% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Epsin 1 | protein | 140 | 71% helix, 1% strand | F1Q523 |
| B | Epsin 1 | protein | 136 | 74% helix, 1% strand | F1Q523 |
| C | Epsin 1 | protein | 138 | 75% helix, 1% strand | F1Q523 |
| D | Epsin 1 | protein | 134 | 75% helix, 1% strand | F1Q523 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 2 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 577 | 0.74 | 0.81 | 58 | empty |
| 2 | 703 | 0.72 | 0.79 | 67 | empty |
| 3 | 148 | 0.60 | 0.84 | 25 | PO4 |
| 4 | 265 | 0.52 | 0.75 | 24 | empty |
Interfaces
5 interfaces between chains.
- C–D · 706 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 543 Ų buried · 4 hydrogen bonds · protein-protein
- A–D · 253 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 139 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 123 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 5LP0 · Crystal structure of the zebra fish enth domain from EPSIN1 in 1.41 ångström resolution · 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 F1Q523
- Elsewhere: RCSB PDB 5LP0 · PDBe 5LP0 · UniProt F1Q523
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