Research workbench
Allosteric peptidic inhibitor of human thymidylate synthase that stabilizes inactive conformation of the enzyme.
Analyse Allosteric peptidic inhibitor of human thymidylate synthase that stabilizes… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FGT
- Type
- protein
- Length
- 271 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thymidylate synthase; Cg peptide
- EC
- 2.1.1.45
- UniProt
- P04818
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thymidylate synthase (EC 2.1.1.45) | protein | 267 | 33% helix, 25% strand | P04818 |
| D | Cg peptide | protein | 4 | 0% helix, 0% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 602 | 0.68 | 0.77 | 53 | empty |
| 2 | 95 | 0.40 | 0.77 | 14 | empty |
| 3 | 58 | 0.28 | 0.73 | 15 | empty |
Interfaces
1 interface between chains.
- A–D · 186 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 2 modified, 1 disulfide (artifact, disulfide).
Compared structures
- 4FGT · Allosteric peptidic inhibitor of human thymidylate synthase that stabilizes inactive… · 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 P04818
- Elsewhere: RCSB PDB 4FGT · PDBe 4FGT · UniProt P04818
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