MolNFT v2 · #48389 · protein
The structures of apo- and inhibitor bound human dihydroorotate dehydrogenase reveal conformational flexibility within the inhibitor binding site
2PRH: “The structures of apo- and inhibitor bound human dihydroorotate dehydrogenase reveal conformational…”. X-ray diffraction at 2.4. MolNFT v2 #48389 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2PRH
- Type
- protein
- Length
- 358 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.4
- Source
- Homo sapiens
- UniProt
- Q02127
Structure
x-ray diffraction · resolution 2.4 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 358 | — | Q02127 |
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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