Research workbench
The crystal structure of a novel, latent dihydroorotase from aquifex aeolicus at 1.7 a resolution
Analyse The crystal structure of a novel, latent dihydroorotase from aquifex aeolicus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1XRT
- Type
- protein
- Length
- 738 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O66990
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 369 | — | O66990 |
| B | — | protein | 369 | — | O66990 |
Compared structures
- 1XRT · The Crystal Structure of a Novel, Latent Dihydroorotase from Aquifex Aeolicus at 1.7 A… · the same entry in another collection · chain A against A, TM-score 1.00
- O66990 · AlphaFold monomer V2.0 prediction for dihydroorotase (O66990) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 O66990
- Elsewhere: RCSB PDB 1XRT · PDBe 1XRT · UniProt O66990
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