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High resolution crystal structure of FOX1 rrm
Analyse High resolution crystal structure of FOX1 rrm in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ZKA
- Type
- protein
- Length
- 484 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA binding protein fox-1 homolog 1
- UniProt
- Q9NWB1
- Ligands
- SO4
- Pockets
- 5 · best druggability 0.48
Structure
x-ray diffraction · 5 distinct chains · 26% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | RNA binding protein fox-1 homolog 1 | protein | 83 | 24% helix, 40% strand | Q9NWB1 |
| C | RNA binding protein fox-1 homolog 1 | protein | 77 | 26% helix, 43% strand | Q9NWB1 |
| D | RNA binding protein fox-1 homolog 1 | protein | 82 | 27% helix, 40% strand | Q9NWB1 |
| E | RNA binding protein fox-1 homolog 1 | protein | 80 | 28% helix, 41% strand | Q9NWB1 |
| F | RNA binding protein fox-1 homolog 1 | protein | 79 | 25% helix, 42% strand | Q9NWB1 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 7 copies · chains A, B, C, D, E, F
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 4 copies · chains A, C, E, F
- PG4 · Tetraethylene glycol · additive · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 90 | 0.48 | 0.81 | 21 | empty |
| 2 | 143 | 0.41 | 0.74 | 22 | SO4 |
| 3 | 56 | 0.33 | 0.77 | 12 | empty |
| 4 | 62 | 0.29 | 0.74 | 11 | empty |
| 5 | 60 | 0.27 | 0.73 | 9 | empty |
Interfaces
8 interfaces between chains.
- D–E · 566 Ų buried · 13 hydrogen bonds · protein-protein
- B–E · 490 Ų buried · 9 hydrogen bonds · protein-protein
- C–E · 306 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 299 Ų buried · 3 hydrogen bonds · protein-protein
- C–F · 248 Ų buried · 6 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 Q9NWB1
- Elsewhere: RCSB PDB 4ZKA · PDBe 4ZKA · UniProt Q9NWB1
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