Research workbench
Structure of viral flavin-dependant thymidylate synthase thyx
Analyse Structure of viral flavin-dependant thymidylate synthase thyx in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CFA
- Type
- protein
- Length
- 359 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thymidylate synthase
- EC
- 2.1.1.148
- UniProt
- O41156
- Ligands
- FAD
- Pockets
- 1 · best druggability 0.43
Structure
x-ray diffraction · 2 distinct chains · 53% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thymidylate synthase (EC 2.1.1.148) | protein | 180 | 53% helix, 18% strand | O41156 |
| B | Thymidylate synthase (EC 2.1.1.148) | protein | 179 | 53% helix, 17% strand | O41156 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 154 | 0.43 | 0.75 | 28 | empty |
Interfaces
1 interface between chains.
- A–B · 1262 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (artifact).
Compared structures
- 2CFA · Structure of viral flavin-dependant thymidylate synthase ThyX · 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 O41156
- Elsewhere: RCSB PDB 2CFA · PDBe 2CFA · UniProt O41156
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