Research workbench
The crystal structure of the complex of LIP5 ntd and IST1 mim
Analyse The crystal structure of the complex of LIP5 ntd and IST1 mim in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4U7E
- Type
- protein
- Length
- 177 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vacuolar protein sorting-associated protein VTA1 homolog; IST1 homolog
- UniProt
- Q9NP79, P53990
Structure
x-ray diffraction · 2 distinct chains · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Vacuolar protein sorting-associated protein VTA1 homolog | protein | 163 | 78% helix, 0% strand | Q9NP79 |
| A | IST1 homolog | protein | 14 | 64% helix, 0% strand | P53990 |
Interfaces
1 interface between chains.
- B–A · 570 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 4U7E · The crystal structure of the complex of LIP5 NTD and IST1 MIM · the same entry in another collection · chain B against B, TM-score 1.00
- Q9NP79 · AlphaFold monomer V2.0 prediction for vacuolar protein sorting- associated protein VTA1… · a predicted model of the same protein · chain B against A, TM-score 0.98
- P53990 · AlphaFold monomer V2.0 prediction for IST1 homolog (P53990) · a predicted model of the same protein · chain A against A, TM-score 0.71
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
- Every structure of UniProt P53990
- Elsewhere: RCSB PDB 4U7E · PDBe 4U7E · UniProt Q9NP79 · UniProt P53990
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.