Research workbench
Structure of SPF45 uhm bound to HIV-1 rev ulm
Analyse Structure of SPF45 uhm bound to HIV-1 rev ulm in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HIP
- Type
- protein
- Length
- 217 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Splicing factor 45; HIV-1 rev (41-49)
- UniProt
- Q96I25
- Ligands
- TRP, NA
- Pockets
- 2 · best druggability 0.36
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Splicing factor 45 | protein | 104 | 29% helix, 25% strand | Q96I25 |
| C | HIV-1 rev (41-49) | protein | 9 | 0% helix, 11% 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 | 74 | 0.36 | 0.76 | 14 | TRP |
| 2 | 58 | 0.33 | 0.77 | 13 | empty |
Interfaces
3 interfaces between chains.
- A–C · 787 Ų buried · 22 hydrogen bonds · protein-protein
- A–B · 345 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 294 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
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 Q96I25
- Elsewhere: RCSB PDB 6HIP · PDBe 6HIP · UniProt Q96I25
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