MolNFT v1 · #157560 · protein
Structure of HIV tat-specific factor 1 U2AF homology motif bound to SF3B1 ULM5
6N3F: “Structure of HIV tat-specific factor 1 U2AF homology motif bound to SF3B1 ULM5”. X-ray diffraction, 2 pockets (best druggability 0.49). MolNFT v1 #157560 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6N3F
- Type
- protein
- Length
- 193 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HIV tat-specific factor 1; SF3B1 U2AF ligand motif
- UniProt
- O43719
- Pockets
- 2 · best druggability 0.49
Structure
x-ray diffraction · 3 distinct chains · 29% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | HIV tat-specific factor 1 | protein | 95 | 29% helix, 27% strand | O43719 |
| C | HIV tat-specific factor 1 | protein | 94 | 30% helix, 28% strand | O43719 |
| D | SF3B1 U2AF ligand motif | protein | 4 | 0% helix, 25% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 223 | 0.49 | 0.75 | 33 | empty |
| 2 | 80 | 0.47 | 0.81 | 11 | empty |
Interfaces
3 interfaces between chains.
- C–D · 392 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 183 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 86 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6N3F · Structure of HIV Tat-specific factor 1 U2AF Homology Motif bound to SF3b1 ULM5 · 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 C 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 6N3F · PDBe 6N3F · UniProt O43719
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