Research workbench
Candida albicans dihydrofolate reductase complexed with NADPH and 5- {3-[3-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-METHOXYPHENYL]PROP-1-yn-1- yl}-6-ethylpyrimidine-2,4-diamine (UCP1018)
Analyse Candida albicans dihydrofolate reductase complexed with NADPH and 5… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4H96
- Type
- protein
- Length
- 378 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydrofolate reductase
- EC
- 1.5.1.3
- UniProt
- Q5A5E0
- Ligands
- NDP, 14Q
- Pockets
- 2 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 22% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Dihydrofolate reductase (EC 1.5.1.3) | protein | 189 | 22% helix, 35% strand | Q5A5E0 |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- 14Q · 5-{3-[3-(1,3-benzodioxol-5-yl)-5-methoxyphenyl]prop-1-yn-1-yl}-6-ethylpyrimidine-2,4-diamine · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1198 | 0.74 | 0.77 | 84 | NDP, 14Q |
| 2 | 565 | 0.70 | 0.79 | 48 | NDP, 14Q |
Interfaces
1 interface between chains.
- A–B · 204 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 4H96 · Candida albicans dihydrofolate reductase complexed with NADPH and… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q5A5E0
- Elsewhere: RCSB PDB 4H96 · PDBe 4H96 · UniProt Q5A5E0
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