Research workbench
Crystal structure of trypanosoma cruzi dihydrofolate reductase- thymidylate synthase in complex with (6S)-5,6,7,8-tetrahydrofolate
Analyse Crystal structure of trypanosoma cruzi dihydrofolate reductase- thymidylate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5T7O
- Type
- protein
- Length
- 1,965 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional dihydrofolate reductase-thymidylate synthase
- UniProt
- Q4DLS1
- Ligands
- NAP, THG, UMP
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 4 distinct chains · 31% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional dihydrofolate reductase-thymidylate synthase | protein | 494 | 31% helix, 27% strand | Q4DLS1 |
| B | Bifunctional dihydrofolate reductase-thymidylate synthase | protein | 495 | 31% helix, 27% strand | Q4DLS1 |
| C | Bifunctional dihydrofolate reductase-thymidylate synthase | protein | 487 | 31% helix, 27% strand | Q4DLS1 |
| D | Bifunctional dihydrofolate reductase-thymidylate synthase | protein | 489 | 30% helix, 27% strand | Q4DLS1 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 4 copies · chains A, B, C, D
- THG · (6S)-5,6,7,8-tetrahydrofolate · ligand · 4 copies · chains A, B, C, D
- UMP · 2'-deoxyuridine 5'-monophosphate · ligand · 4 copies · chains A, B, C, D
- EDO · 1,2-ethanediol · additive · 47 copies · chains A, B, D, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1091 | 0.82 | 0.83 | 104 | EDO |
| 2 | 758 | 0.82 | 0.85 | 77 | EDO |
| 3 | 758 | 0.82 | 0.85 | 73 | empty |
| 4 | 740 | 0.81 | 0.85 | 77 | EDO |
| 5 | 663 | 0.69 | 0.77 | 40 | EDO |
Interfaces
6 interfaces between chains.
- C–D · 2060 Ų buried · 27 hydrogen bonds · protein-protein
- A–B · 2050 Ų buried · 27 hydrogen bonds · protein-protein
- B–C · 1029 Ų buried · 16 hydrogen bonds · protein-protein
- A–D · 963 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 752 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 5T7O · Crystal structure of Trypanosoma cruzi Dihydrofolate Reductase-Thymidylate Synthase in… · 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 Q4DLS1
- Elsewhere: RCSB PDB 5T7O · PDBe 5T7O · UniProt Q4DLS1
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.