MolNFT v1 · #114829 · protein
Structure of the IMP2 F-bar domain
5C1F · Septation protein IMP2: “Structure of the IMP2 F-bar domain”. X-ray diffraction, 3 pockets (best druggability 0.42). MolNFT v1 #114829 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5C1F
- Type
- protein
- Length
- 596 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Septation protein IMP2
- UniProt
- Q10199
- Pockets
- 3 · best druggability 0.42
Structure
x-ray diffraction · 1 distinct chain · 81% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Septation protein IMP2 | protein | 298 | 81% helix, 3% strand | Q10199 |
Ligands and binding sites
- FMT · Formic acid · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 123 | 0.42 | 0.76 | 24 | empty |
| 2 | 105 | 0.41 | 0.77 | 23 | empty |
| 3 | 53 | 0.30 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 6080 Ų buried · 87 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 Q10199
- Elsewhere: RCSB PDB 5C1F · PDBe 5C1F · UniProt Q10199
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