MolNFT v1 · #21241 · protein
Structure determination of tetrahydroquinazoline antifolates in complex with human and pneumocystis carinii dihydrofolate reductase: correlations of enzyme selectivity and stereochemistry
1S3U: “Structure determination of tetrahydroquinazoline antifolates in complex with human and pneumocystis carinii…”. X-ray diffraction. MolNFT v1 #21241 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1S3U
- Type
- protein
- Length
- 186 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00374
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 186 | — | P00374 |
Compared structures
- 1S3U · 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 1S3U · PDBe 1S3U · UniProt P00374
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