Research workbench
Crystal structure of the A287F/S290G active site mutant of ts-DHFR from cryptosporidium hominis
Analyse Crystal structure of the A287F/S290G active site mutant of ts-DHFR from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3DL6
- Type
- protein
- Length
- 2,536 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydrofolate reductase, DHFR
- EC
- 1.5.1.3
- UniProt
- Q5CGA3
- Ligands
- UMP, CB3, DHF, NDP
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 3 distinct chains · 28% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydrofolate reductase, DHFR (EC 1.5.1.3) | protein | 505 | 28% helix, 26% strand | Q5CGA3 |
| B, C, D | Dihydrofolate reductase, DHFR (EC 1.5.1.3) | protein | 508 | 28% helix, 25% strand | Q5CGA3 |
| E | Dihydrofolate reductase, DHFR (EC 1.5.1.3) | protein | 507 | 29% helix, 24% strand | Q5CGA3 |
Ligands and binding sites
- UMP · 2'-deoxyuridine 5'-monophosphate · ligand · 5 copies · chains A, B, C, D, E
- CB3 · 10-propargyl-5,8-dideazafolic acid · ligand · 5 copies · chains A, B, C, D, E
- DHF · Dihydrofolic acid · 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, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 459 | 0.79 | 0.86 | 48 | UMP, CB3 |
| 2 | 426 | 0.78 | 0.87 | 47 | UMP, CB3 |
| 3 | 455 | 0.78 | 0.86 | 47 | UMP, CB3 |
| 4 | 407 | 0.77 | 0.86 | 41 | UMP, CB3 |
| 5 | 508 | 0.76 | 0.84 | 46 | UMP, CB3 |
Interfaces
2 interfaces between chains.
- C–D · 4298 Ų buried · 60 hydrogen bonds · protein-protein
- A–B · 4205 Ų buried · 62 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 3DL6 · Crystal Structure of the A287F/S290G Active Site Mutant of TS-DHFR 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 Q5CGA3
- Elsewhere: RCSB PDB 3DL6 · PDBe 3DL6 · UniProt Q5CGA3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.