Research workbench
Crystal structure of hepatitis B X-interacting protein at high resolution
Analyse Crystal structure of hepatitis B X-interacting protein at high resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MSH
- Type
- protein
- Length
- 90 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hepatitis B virus X-interacting protein
- UniProt
- O43504
- Ligands
- PO4
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hepatitis B virus X-interacting protein | protein | 90 | 28% helix, 37% strand | O43504 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
- IPA · Isopropyl alcohol · additive · 3 copies · chains A
- GOL · Glycerol · additive · chains A
- PG4 · Tetraethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3MSH · Crystal structure of Hepatitis B X-Interacting Protein at high resolution · the same entry in another collection · chain A against A, TM-score 1.00
- 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 0.91
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
- Elsewhere: RCSB PDB 3MSH · PDBe 3MSH · UniProt O43504
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