MolNFT v1 · #48380 · protein
The structures of apo- and inhibitor bound human dihydroorotate dehydrogenase reveal conformational flexibility within the inhibitor binding site
2PRH · Dihydroorotate dehydrogenase, mitochondrial: “The structures of apo- and inhibitor bound human dihydroorotate dehydrogenase reveal conformational…”. X-ray diffraction, 4 ligands (FMN, ORO, 238), 4 pockets (best druggability 0.83).…
- PDB
- 2PRH
- Type
- protein
- Length
- 358 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydroorotate dehydrogenase, mitochondrial
- EC
- 1.3.99.11
- UniProt
- Q02127
- Ligands
- FMN, ORO, 238, DDQ
- Pockets
- 4 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydroorotate dehydrogenase, mitochondrial (EC 1.3.99.11) | protein | 358 | 45% helix, 16% strand | Q02127 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · chains A
- ORO · Orotic acid · ligand · chains A
- 238 · 6-chloro-2-(2'-fluorobiphenyl-4-yl)-3-methylquinoline-4-carboxylic acid · ligand · chains A
- DDQ · Decylamine-N,N-dimethyl-N-oxide · ligand · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 587 | 0.83 | 0.88 | 79 | FMN, ORO, 238, DDQ |
| 2 | 118 | 0.47 | 0.79 | 19 | empty |
| 3 | 54 | 0.41 | 0.82 | 17 | empty |
| 4 | 83 | 0.40 | 0.78 | 18 | empty |
Compared structures
- 2PRH · The structures of apo- and inhibitor bound human dihydroorotate dehydrogenase reveal… · 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 Q02127
- Elsewhere: RCSB PDB 2PRH · PDBe 2PRH · UniProt Q02127
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