Research workbench
Structures of thymidylate synthase with a C-terminal deletion: role of the C-terminus in alignment of D/UMP and CH2H4FOLATE
Analyse Structures of thymidylate synthase with a C-terminal deletion: role of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2TDD
- Type
- protein
- Length
- 315 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thymidylate synthase
- EC
- 2.1.1.45
- UniProt
- P00469
- Ligands
- THF, UFP
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thymidylate synthase (EC 2.1.1.45) | protein | 315 | 37% helix, 21% strand | P00469 |
Ligands and binding sites
- THF · 5-hydroxymethylene-6-hydrofolic acid · ligand · chains A
- UFP · 5-fluoro-2'-deoxyuridine-5'-monophosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 817 | 0.72 | 0.77 | 60 | THF, UFP |
| 2 | 78 | 0.53 | 0.85 | 16 | empty |
Compared structures
- 2TDD · Structures of thymidylate synthase with a C-terminal deletion: role of the C-terminus in… · the same entry in another collection · chain A against A, TM-score 1.00
- P00469 · AlphaFold monomer V2.0 prediction for thymidylate synthase (P00469) · 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 P00469
- Elsewhere: RCSB PDB 2TDD · PDBe 2TDD · UniProt P00469
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