Research workbench
Crystal structure of C7ORF59-hbxip complex
Analyse Crystal structure of C7ORF59-hbxip complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5Y38
- Type
- protein
- Length
- 162 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ragulator complex protein LAMTOR5; Ragulator complex protein LAMTOR4
- UniProt
- O43504, Q0VGL1
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.36
Structure
x-ray diffraction · 2 distinct chains · 22% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ragulator complex protein LAMTOR5 | protein | 84 | 25% helix, 38% strand | O43504 |
| B | Ragulator complex protein LAMTOR4 | protein | 78 | 19% helix, 46% strand | Q0VGL1 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 66 | 0.36 | 0.77 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1036 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 5Y38 · Crystal structure of C7orf59-HBXIP complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q0VGL1 · AlphaFold monomer V2.0 prediction for ragulator complex protein LAMTOR4 (Q0VGL1) · a predicted model of the same protein · chain B against A, TM-score 0.93
- O43504 · AlphaFold monomer V2.0 prediction for ragulator complex protein LAMTOR5 (O43504) · a predicted model of the same protein · chain A against A, TM-score 0.88
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 O43504
- Every structure of UniProt Q0VGL1
- Elsewhere: RCSB PDB 5Y38 · PDBe 5Y38 · UniProt O43504 · UniProt Q0VGL1
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