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The crystal structure of the T109S mutant of E. COLI dihydroorotase complexed with an inhibitor 5-fluoroorotate
Analyse The crystal structure of the T109S mutant of E. COLI dihydroorotase complexed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2E25
- Type
- protein
- Length
- 343 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydroorotase
- EC
- 3.5.2.3
- UniProt
- P05020
- Ligands
- FOT, ZN
- Pockets
- 3 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydroorotase (EC 3.5.2.3) | protein | 343 | 37% helix, 17% strand | P05020 |
Ligands and binding sites
- FOT · 5-fluoro-2,6-dioxo-1,2,3,6-tetrahydropyrimidine-4-carboxylic acid · ligand · chains A
- ZN · Zinc ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 131 | 0.48 | 0.78 | 22 | empty |
| 2 | 188 | 0.47 | 0.75 | 28 | FOT |
| 3 | 52 | 0.28 | 0.75 | 13 | empty |
Modifications
Observed in the structure: 1 modified (carboxylation).
Compared structures
- 2E25 · The Crystal Structure of the T109S mutant of E. coli Dihydroorotase complexed with an… · the same entry in another collection · chain A against A, TM-score 1.00
- P05020 · AlphaFold monomer V2.0 prediction for dihydroorotase (P05020) · a predicted model of the same protein · chain A 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 P05020
- Elsewhere: RCSB PDB 2E25 · PDBe 2E25 · UniProt P05020
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