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Crystal structure of dihydrofolate reductase-thymidylate synthase from cryptosporidium hominis bound to 1843U89/NADPH/DUMP
Analyse Crystal structure of dihydrofolate reductase-thymidylate synthase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SEJ
- Type
- protein
- Length
- 2,595 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional dihydrofolate reductase-thymidylate synthase
- EC
- 2.1.1.45, 1.5.1.3
- UniProt
- Q27552
- Ligands
- F89, UMP, NDP
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Bifunctional dihydrofolate reductase-thymidylate synthase (EC 2.1.1.45, 1.5.1.3) | protein | 519 | 28% helix, 25% strand | Q27552 |
Ligands and binding sites
- F89 · S)-2-(5(((1,2-dihydro-3-methyl-1-oxobenzo(f)quinazolin-9-yl)methyl)amino)1-oxo-2-isoindolinyl)glutaric acid · ligand · 10 copies · chains A, B, C, D, E
- UMP · 2'-deoxyuridine 5'-monophosphate · ligand · 5 copies · chains A, B, C, D, E
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 5 copies · chains A, B, C, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 998 | 0.82 | 0.83 | 84 | empty |
| 2 | 1027 | 0.82 | 0.83 | 83 | empty |
| 3 | 459 | 0.79 | 0.87 | 49 | UMP, F89 |
| 4 | 423 | 0.79 | 0.87 | 48 | UMP, F89 |
| 5 | 464 | 0.79 | 0.86 | 50 | UMP, F89 |
Interfaces
2 interfaces between chains.
- A–B · 4400 Ų buried · 76 hydrogen bonds · protein-protein
- C–D · 4376 Ų buried · 76 hydrogen bonds · protein-protein
Compared structures
- 1SEJ · Crystal Structure of Dihydrofolate Reductase-Thymidylate Synthase from Cryptosporidium… · 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 Q27552
- Elsewhere: RCSB PDB 1SEJ · PDBe 1SEJ · UniProt Q27552
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