Research workbench
Toxoplasma gondii dihydrofolate reductase thymidylate synthase (tgdhfr-ts) complexed with P40, NADPH and dump
Analyse Toxoplasma gondii dihydrofolate reductase thymidylate synthase (tgdhfr-ts)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7FGY
- Type
- protein
- Length
- 2,240 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q07422
- Ligands
- NDP, 4TS, UMP
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 559 | — | Q07422 |
| B, D | — | protein | 562 | — | Q07422 |
| C | — | protein | 557 | — | Q07422 |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 4 copies · chains A, B, C, D
- 4TS · 5-(3-chlorophenyl)-6-[2-(3-phenoxypropoxy) ethyl]pyrimidine-2,4-diamine · ligand · 4 copies · chains A, B, C, D
- UMP · 2'-deoxyuridine 5'-monophosphate · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- Q07422 · AlphaFold monomer V2.0 prediction for bifunctional dihydrofolate reductase-thymidylate… · a predicted model of the same protein · chain C against A, TM-score 0.95
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 Q07422
- Elsewhere: RCSB PDB 7FGY · PDBe 7FGY · UniProt Q07422
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