Research workbench
Structure of SF1 coiled-coil domain
Analyse Structure of SF1 coiled-coil domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FXX
- Type
- protein
- Length
- 365 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Splicing factor 1
- UniProt
- Q15637
- Pockets
- 5 · best druggability 0.57
Structure
x-ray diffraction · 4 distinct chains · 50% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Splicing factor 1 | protein | 93 | 47% helix, 2% strand | Q15637 |
| B | Splicing factor 1 | protein | 86 | 52% helix, 2% strand | Q15637 |
| C | Splicing factor 1 | protein | 91 | 48% helix, 4% strand | Q15637 |
| D | Splicing factor 1 | protein | 95 | 52% helix, 1% strand | Q15637 |
Ligands and binding sites
- IMD · Imidazole · additive · 8 copies · chains A, B, C, D
- MLI · Malonate ion · additive · 2 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 247 | 0.57 | 0.78 | 35 | MLI |
| 2 | 130 | 0.41 | 0.75 | 27 | empty |
| 3 | 68 | 0.31 | 0.75 | 11 | IMD |
| 4 | 53 | 0.28 | 0.74 | 13 | empty |
| 5 | 58 | 0.27 | 0.74 | 13 | empty |
Interfaces
5 interfaces between chains.
- A–B · 972 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 343 Ų buried · 3 hydrogen bonds · protein-protein
- C–D · 170 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 97 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 32 Ų buried · 0 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 Q15637
- Elsewhere: RCSB PDB 4FXX · PDBe 4FXX · UniProt Q15637
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