MolNFT v1 · #36517 · protein
Crystal structure of an orotidine-5'-monophosphate decarboxylase homolog from P.FALCIPARUM
2F84 · Orotidine monophosphate decarboxylase: “Crystal structure of an orotidine-5'-monophosphate decarboxylase homolog from P.FALCIPARUM”. X-ray diffraction, 1 ligand (PO4), 4 pockets (best druggability 0.46). MolNFT v1 #36517 on…
- PDB
- 2F84
- Type
- protein
- Length
- 323 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Orotidine monophosphate decarboxylase
- EC
- 4.1.1.23
- UniProt
- Q8IJH3
- Ligands
- PO4
- Pockets
- 4 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 56% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Orotidine monophosphate decarboxylase (EC 4.1.1.23) | protein | 323 | 56% helix, 14% strand | Q8IJH3 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 129 | 0.46 | 0.78 | 22 | empty |
| 2 | 85 | 0.41 | 0.78 | 19 | empty |
| 3 | 99 | 0.40 | 0.77 | 14 | empty |
| 4 | 95 | 0.36 | 0.75 | 25 | PO4 |
Compared structures
- 2F84 · Crystal Structure of an orotidine-5'-monophosphate decarboxylase homolog from P.falciparum · 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 Q8IJH3
- Elsewhere: RCSB PDB 2F84 · PDBe 2F84 · UniProt Q8IJH3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.