MolNFT v1 · #4185 · protein
Factor D inhibited by diisopropyl fluorophosphate
1DFP: “Factor D inhibited by diisopropyl fluorophosphate”. X-ray diffraction, 1 ligand (DFP), 4 pockets (best druggability 0.63). MolNFT v1 #4185 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1DFP
- Type
- protein
- Length
- 456 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Factor D
- EC
- 3.4.21.46
- UniProt
- P00746
- Ligands
- DFP
- Pockets
- 4 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Factor D (EC 3.4.21.46) | protein | 228 | 8% helix, 36% strand | P00746 |
Ligands and binding sites
- DFP · Diisopropyl phosphonate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 432 | 0.63 | 0.77 | 56 | empty |
| 2 | 177 | 0.52 | 0.78 | 31 | DFP |
| 3 | 159 | 0.49 | 0.77 | 32 | empty |
| 4 | 97 | 0.40 | 0.77 | 21 | DFP |
Interfaces
1 interface between chains.
- A–B · 854 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide, 2 covalent (disulfide, covalent ligand).
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 P00746
- Elsewhere: RCSB PDB 1DFP · PDBe 1DFP · UniProt P00746
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