MolNFT v1 · #168384 · protein
Crystal structure of ts-DHFR from cryptosporidium hominis with apo-ts site
6WEP · Bifunctional dihydrofolate reductase-thymidylate synthase: “Crystal structure of ts-DHFR from cryptosporidium hominis with apo-ts site”. X-ray diffraction, 2 ligands (NDP, MTX), 15 pockets (best druggability 0.74). MolNFT v1 #168384…
- PDB
- 6WEP
- Type
- protein
- Length
- 1,006 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional dihydrofolate reductase-thymidylate synthase
- UniProt
- A0A0S4TER9
- Ligands
- NDP, MTX
- Pockets
- 15 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Bifunctional dihydrofolate reductase-thymidylate synthase | protein | 503 | 27% helix, 26% strand | A0A0S4TER9 |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- MTX · Methotrexate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 657 | 0.74 | 0.80 | 58 | empty |
| 2 | 693 | 0.72 | 0.78 | 46 | empty |
| 3 | 1187 | 0.71 | 0.75 | 84 | empty |
| 4 | 344 | 0.69 | 0.82 | 34 | NDP, MTX |
| 5 | 355 | 0.69 | 0.82 | 36 | NDP, MTX |
Interfaces
1 interface between chains.
- A–B · 4186 Ų buried · 73 hydrogen bonds · protein-protein
Compared structures
- 6WEP · Crystal structure of TS-DHFR from Cryptosporidium hominis with Apo-TS site · 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 A0A0S4TER9
- Elsewhere: RCSB PDB 6WEP · PDBe 6WEP · UniProt A0A0S4TER9
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