Research workbench
Ternary complex between E. COLI thymidylate synthase, dump, and F9
Analyse Ternary complex between E. COLI thymidylate synthase, dump, and F9 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LRR
- Type
- protein
- Length
- 264 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thymidylate synthase
- EC
- 2.1.1.45
- UniProt
- P0A886
- Ligands
- ACE, CF9, UMP, SO4
- Pockets
- 1 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thymidylate synthase (EC 2.1.1.45) | protein | 264 | 34% helix, 27% strand | P0A886 |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains A
- CF9 · 2-oxo-2H-naphtho[1,8-bc]furan-6-yl 4-nitrobenzoate · ligand · chains A
- UMP · 2'-deoxyuridine 5'-monophosphate · ligand · chains A
- SO4 · Sulfate ion · ion · 8 copies · 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 | 582 | 0.70 | 0.78 | 47 | SO4, CF9 |
Modifications
Observed in the structure: 1 covalent, 1 modified (covalent ligand, methylation).
Compared structures
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 P0A886
- Elsewhere: RCSB PDB 4LRR · PDBe 4LRR · UniProt P0A886
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