MolNFT v1 · #106695 · protein
Plastic adaptation toward mutations in proteins: structural comparison of thymidylate synthases
4TMS: “Plastic adaptation toward mutations in proteins: structural comparison of thymidylate synthases”. X-ray diffraction, 1 ligand (PO4), 1 pocket (best druggability 0.75). MolNFT v1 #106695 on GenesisL1: 3D structure, binding sites and…
- PDB
- 4TMS
- Type
- protein
- Length
- 316 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
- PO4
- Pockets
- 1 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thymidylate synthase (EC 2.1.1.45) | protein | 316 | 41% helix, 22% strand | P00469 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 894 | 0.75 | 0.78 | 60 | PO4 |
Compared structures
- 4TMS · Plastic adaptation toward mutations in proteins: structural comparison of thymidylate… · 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 P00469
- Elsewhere: RCSB PDB 4TMS · PDBe 4TMS · UniProt P00469
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