Research workbench
Crystal structure of the zebra fish enth domain from EPSIN1 in 1.41 ångström resolution
Analyse Crystal structure of the zebra fish enth domain from EPSIN1 in 1.41 ångström… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- 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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