Research workbench
Mouse thymidylate synthase in ternary complex with fdump and methylenetetrahydrofolate.
Analyse Mouse thymidylate synthase in ternary complex with fdump and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FCT
- Type
- protein
- Length
- 574 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thymidylate synthase
- UniProt
- Q544L2
- Ligands
- UFP, C2F
- Pockets
- 7 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Thymidylate synthase | protein | 287 | 34% helix, 23% strand | Q544L2 |
Ligands and binding sites
- UFP · 5-fluoro-2'-deoxyuridine-5'-monophosphate · ligand · 2 copies · chains A, B
- C2F · 5-methyl-5,6,7,8-tetrahydrofolic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 409 | 0.77 | 0.86 | 47 | UFP, C2F |
| 2 | 377 | 0.76 | 0.86 | 42 | UFP, C2F |
| 3 | 177 | 0.52 | 0.78 | 22 | empty |
| 4 | 153 | 0.48 | 0.77 | 26 | empty |
| 5 | 75 | 0.37 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 2183 Ų buried · 36 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 5FCT · Mouse thymidylate synthase in ternary complex with FdUMP and methylenetetrahydrofolate. · 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 Q544L2
- Elsewhere: RCSB PDB 5FCT · PDBe 5FCT · UniProt Q544L2
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