Research workbench
Crystal structure of the TSG101 uev domain in complex with FA459 peptide
Analyse Crystal structure of the TSG101 uev domain in complex with FA459 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3P9G
- Type
- protein
- Length
- 149 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tumor susceptibility gene 101 protein; Gag polyprotein
- UniProt
- Q99816, Q9YP46
- Ligands
- ACE, NH2
Structure
x-ray diffraction · 2 distinct chains · 26% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tumor susceptibility gene 101 protein | protein | 140 | 28% helix, 34% strand | Q99816 |
| B | Gag polyprotein | protein | 9 | 0% helix, 11% strand | Q9YP46 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 736 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent, 1 modified (covalent ligand, nonstandard).
Compared structures
- 3P9G · Crystal structure of the TSG101 UEV domain in complex with FA459 peptide · the same entry in another collection · chain A against A, TM-score 1.00
- Q99816 · AlphaFold monomer V2.0 prediction for tumor susceptibility gene 101 protein (Q99816) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q99816
- Every structure of UniProt Q9YP46
- Elsewhere: RCSB PDB 3P9G · PDBe 3P9G · UniProt Q99816 · UniProt Q9YP46
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