MolNFT v1 · #21242 · protein
Structure determination of tetrahydroquinazoline antifolates in complex with human and pneumocystis carinii dihydrofolate reductase: correlations of enzyme selectivity and stereochemistry
1S3V: “Structure determination of tetrahydroquinazoline antifolates in complex with human and pneumocystis carinii…”. X-ray diffraction, 2 ligands (TQD, SO4), 3 pockets (best druggability 0.75). MolNFT v1 #21242 on GenesisL1: 3D structure…
- PDB
- 1S3V
- 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
- P00374
- Ligands
- TQD, SO4
- Pockets
- 3 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 21% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydrofolate reductase (EC 1.5.1.3) | protein | 186 | 21% helix, 32% strand | P00374 |
Ligands and binding sites
- TQD · (2R,6S)-6-{[methyl(3,4,5-trimethoxyphenyl)amino]methyl}-1,2,5,6,7,8-hexahydroquinazoline-2,4-diamine · ligand · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 385 | 0.75 | 0.85 | 44 | SO4, TQD |
| 2 | 55 | 0.31 | 0.76 | 13 | empty |
| 3 | 60 | 0.29 | 0.75 | 16 | empty |
Compared structures
- 1S3V · Structure Determination of Tetrahydroquinazoline Antifolates in Complex with Human and… · the same entry in another collection · chain A against A, TM-score 1.00
- P00374 · AlphaFold monomer V2.0 prediction for dihydrofolate reductase (P00374) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P00374
- Elsewhere: RCSB PDB 1S3V · PDBe 1S3V · UniProt P00374
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