MolNFT v1 · #37205 · protein
Crystal structure of dihydropyrimidinase from dictyostelium discoideum
2FTW · Dihydropyrimidine amidohydrolase: “Crystal structure of dihydropyrimidinase from dictyostelium discoideum”. X-ray diffraction, 1 ligand (ZN), 2 pockets (best druggability 0.66). MolNFT v1 #37205 on GenesisL1: 3D structure, binding…
- PDB
- 2FTW
- Type
- protein
- Length
- 484 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydropyrimidine amidohydrolase
- EC
- 3.5.2.2
- UniProt
- Q86LT2
- Ligands
- ZN
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydropyrimidine amidohydrolase (EC 3.5.2.2) | protein | 484 | 36% helix, 22% strand | Q86LT2 |
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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 308 | 0.66 | 0.81 | 36 | empty |
| 2 | 57 | 0.41 | 0.82 | 19 | empty |
Modifications
Observed in the structure: 1 modified (carboxylation).
Compared structures
- 2FTW · Crystal structure of dihydropyrimidinase from dictyostelium discoideum · the same entry in another collection · chain A against A, TM-score 1.00
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 Q86LT2
- Elsewhere: RCSB PDB 2FTW · PDBe 2FTW · UniProt Q86LT2
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