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Candida glabrata dihydrofolate reductase complexed with NADPH and 2,4- diamino-5-(3-(2,5-DIMETHOXYPHENYL)PROP-1-ynyl)-6-ethylpyrimidine (UCP120B)
Analyse Candida glabrata dihydrofolate reductase complexed with NADPH and 2,4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CSE
- Type
- protein
- Length
- 450 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydrofolate reductase
- EC
- 1.5.1.3
- UniProt
- Q6FPH0
- Ligands
- NDP, N22
- Pockets
- 4 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Dihydrofolate reductase (EC 1.5.1.3) | protein | 225 | 24% helix, 35% strand | Q6FPH0 |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- N22 · 5-[3-(2,5-dimethoxyphenyl)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
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1058 | 0.82 | 0.83 | 109 | NDP, N22 |
| 2 | 625 | 0.65 | 0.76 | 56 | empty |
| 3 | 59 | 0.40 | 0.80 | 11 | empty |
| 4 | 87 | 0.35 | 0.75 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1238 Ų buried · 30 hydrogen bonds · protein-protein
Compared structures
- 3CSE · Candida glabrata 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 Q6FPH0
- Elsewhere: RCSB PDB 3CSE · PDBe 3CSE · UniProt Q6FPH0
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