Research workbench
Candida albicans dihydrofolate reductase complex in which the dihydronicotinamide moiety of dihydro-nicotinamide-adenine- dinucleotide phosphate (NADPH) is displaced by 5-{[4-(4-morpholinyl) PHENYL]SULFANYL}-2,4-quinazolinediamin (GW2021)
Analyse Candida albicans dihydrofolate reductase complex in which the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1IA4
- Type
- protein
- Length
- 384 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P22906
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 192 | — | P22906 |
Compared structures
- 1IA4 · Candida albicans dihydrofolate reductase complex in which the dihydronicotinamide moiety… · the same entry in another collection · chain A against A, TM-score 1.00
- P22906 · AlphaFold monomer V2.0 prediction for dihydrofolate reductase (P22906) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 P22906
- Elsewhere: RCSB PDB 1IA4 · PDBe 1IA4 · UniProt P22906
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