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Structure of HIV tat-specific factor 1 U2AF homology motif bound to U2AF ligand motif 4
Analyse Structure of HIV tat-specific factor 1 U2AF homology motif bound to U2AF ligand… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6N3E
- Type
- protein
- Length
- 101 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HIV tat-specific factor 1; SF3B1 U2AF ligand motif
- UniProt
- O43719
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | HIV tat-specific factor 1 | protein | 94 | 30% helix, 28% strand | O43719 |
| B | SF3B1 U2AF ligand motif | protein | 7 | 0% helix, 14% strand | — |
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 · 494 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 6N3E · Structure of HIV Tat-specific factor 1 U2AF Homology Motif bound to U2AF ligand motif 4 · the same entry in another collection · chain A against A, TM-score 1.00
- O43719 · AlphaFold monomer V2.0 prediction for HIV tat-specific factor 1 (O43719) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 O43719
- Elsewhere: RCSB PDB 6N3E · PDBe 6N3E · UniProt O43719
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