Research workbench
Pneumocystis carinii dihydrofolate reductase ternary complex with NADPH and the inhibitor 24, (N~6~-methyl-N~6~-(naphthalen-1-yl) PYRIDO[2,3-D]PYRIMIDINE-2,4,6-triamine)
Analyse Pneumocystis carinii dihydrofolate reductase ternary complex with NADPH and the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QJZ
- 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
- 33M, NDP
- Pockets
- 1 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D | Dihydrofolate reductase (EC 1.5.1.3) | protein | 206 | 27% helix, 29% strand | P16184 |
Ligands and binding sites
- 33M · N~6~-methyl-N~6~-(naphthalen-1-yl)pyrido[2,3-d]pyrimidine-2,4,6-triamine · ligand · chains D
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 449 | 0.70 | 0.80 | 43 | 33M, NDP |
Compared structures
- 4QJZ · Pneumocystis carinii dihydrofolate reductase ternary complex with NADPH and the inhibitor… · the same entry in another collection · chain D against D, TM-score 1.00
- P16184 · AlphaFold monomer V2.0 prediction for dihydrofolate reductase (P16184) · a predicted model of the same protein · chain D 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 4QJZ · PDBe 4QJZ · UniProt P16184
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