Research workbench
Crystal structure of dihydrofolate REDUCTASE/THYMIDYLATE synthase from babesia bovis determined using slipchip based microfluidics
Analyse Crystal structure of dihydrofolate REDUCTASE/THYMIDYLATE synthase from babesia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3KJR
- Type
- protein
- Length
- 993 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydrofolate REDUCTASE/THYMIDYLATE synthase
- EC
- 2.1.1.45
- UniProt
- A7ASX7
- Ligands
- NAP
- Pockets
- 15 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydrofolate REDUCTASE/THYMIDYLATE synthase (EC 2.1.1.45) | protein | 498 | 30% helix, 25% strand | A7ASX7 |
| B | Dihydrofolate REDUCTASE/THYMIDYLATE synthase (EC 2.1.1.45) | protein | 495 | 29% helix, 26% strand | A7ASX7 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- GOL · Glycerol · additive · 5 copies · chains A, B
- NHE · 2-[N-cyclohexylamino]ethane sulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 314 | 0.76 | 0.87 | 42 | GOL |
| 2 | 536 | 0.74 | 0.82 | 48 | NAP |
| 3 | 704 | 0.73 | 0.79 | 65 | empty |
| 4 | 501 | 0.70 | 0.80 | 48 | NAP |
| 5 | 200 | 0.51 | 0.76 | 20 | GOL |
Interfaces
1 interface between chains.
- A–B · 3130 Ų buried · 38 hydrogen bonds · protein-protein
Compared structures
- 3KJR · Crystal structure of dihydrofolate reductase/thymidylate synthase from Babesia bovis… · 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 A7ASX7
- Elsewhere: RCSB PDB 3KJR · PDBe 3KJR · UniProt A7ASX7
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