Research workbench
New insights into DHFR interactions: analysis of pneumocystis carinii and mouse DHFR complexes with NADPH and two highly potent trimethoprim derivatives
Analyse New insights into DHFR interactions: analysis of pneumocystis carinii and mouse… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FZJ
- Type
- protein
- Length
- 186 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydrofolate reductase
- EC
- 1.5.1.3
- UniProt
- P00375
- Ligands
- NDP, DH3
- Pockets
- 2 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 22% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydrofolate reductase (EC 1.5.1.3) | protein | 186 | 22% helix, 32% strand | P00375 |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- DH3 · 2,4-diamino-5-[3',4'-dimethoxy-5'-(5-carboxyl-1-pentynyl)]benzyl pyrimidine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 514 | 0.73 | 0.81 | 50 | NDP, DH3 |
| 2 | 61 | 0.32 | 0.76 | 13 | empty |
Compared structures
- 2FZJ · New Insights into DHFR Interactions: Analysis of Pneumocystis carinii and Mouse DHFR… · the same entry in another collection · chain A against A, TM-score 1.00
- P00375 · AlphaFold monomer V2.0 prediction for dihydrofolate reductase (P00375) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P00375
- Elsewhere: RCSB PDB 2FZJ · PDBe 2FZJ · UniProt P00375
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