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Crystal structure of LIP5 N-terminal domain
Analyse Crystal structure of LIP5 N-terminal domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4TXP
- Type
- protein
- Length
- 456 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vacuolar protein sorting-associated protein VTA1 homolog
- UniProt
- Q9NP79
- Pockets
- 5 · best druggability 0.77
Structure
x-ray diffraction · 3 distinct chains · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar protein sorting-associated protein VTA1 homolog | protein | 156 | 79% helix, 0% strand | Q9NP79 |
| B | Vacuolar protein sorting-associated protein VTA1 homolog | protein | 153 | 80% helix, 0% strand | Q9NP79 |
| C | Vacuolar protein sorting-associated protein VTA1 homolog | protein | 147 | 78% helix, 0% strand | Q9NP79 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 971 | 0.77 | 0.80 | 82 | empty |
| 2 | 272 | 0.55 | 0.76 | 39 | empty |
| 3 | 164 | 0.50 | 0.78 | 27 | empty |
| 4 | 52 | 0.34 | 0.78 | 13 | empty |
| 5 | 74 | 0.29 | 0.73 | 19 | empty |
Interfaces
3 interfaces between chains.
- B–C · 401 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 391 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 378 Ų buried · 3 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 Q9NP79
- Elsewhere: RCSB PDB 4TXP · PDBe 4TXP · UniProt Q9NP79
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