MolNFT v1 · #37382 · protein
New insights into DHFR interactions: analysis of pneumocystis carinii and mouse DHFR complexes with NADPH and two highly potent trimethoprim derivatives
2FZI · Dihydrofolate reductase: “New insights into DHFR interactions: analysis of pneumocystis carinii and mouse DHFR complexes with NADPH and…”. X-ray diffraction, 2 ligands (NDP, DH3), 2 pockets (best druggability 0.72). MolNFT v1 #37382…
- PDB
- 2FZI
- Type
- protein
- Length
- 206 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydrofolate reductase
- EC
- 1.5.1.3
- UniProt
- P16184
- Ligands
- NDP, DH3
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydrofolate reductase (EC 1.5.1.3) | protein | 206 | 27% helix, 31% strand | P16184 |
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 | 474 | 0.72 | 0.81 | 47 | NDP, DH3 |
| 2 | 52 | 0.30 | 0.76 | 12 | empty |
Compared structures
- 2FZI · 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
- P16184 · AlphaFold monomer V2.0 prediction for dihydrofolate reductase (P16184) · 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 P16184
- Elsewhere: RCSB PDB 2FZI · PDBe 2FZI · UniProt P16184
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