MolNFT v1 · #69132 · protein
Crystal structure of putative dihydrofolate reductase (YP_001636057.1) from chloroflexus aurantiacus J-10-fl at 1.50 a resolution
3KGY · Bifunctional deaminase-reductase domain protein: “Crystal structure of putative dihydrofolate reductase (YP_001636057.1) from chloroflexus aurantiacus J-10-fl…”. X-ray diffraction, 2 ligands (NDP, CL), 5 pockets (best druggability…
- PDB
- 3KGY
- Type
- protein
- Length
- 436 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional deaminase-reductase domain protein
- UniProt
- A9WHX7
- Ligands
- NDP, CL
- Pockets
- 5 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Bifunctional deaminase-reductase domain protein | protein | 218 | 32% helix, 29% strand | A9WHX7 |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- CL · Chloride ion · ion · 2 copies · chains B
- EDO · 1,2-ethanediol · additive · 18 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 727 | 0.79 | 0.83 | 68 | NDP, EDO |
| 2 | 732 | 0.78 | 0.82 | 62 | NDP, EDO |
| 3 | 51 | 0.71 | 0.98 | 24 | EDO |
| 4 | 69 | 0.30 | 0.74 | 17 | EDO |
| 5 | 60 | 0.30 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1125 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 modified (engineered).
Compared structures
- 3KGY · Crystal structure of Putative dihydrofolate reductase (YP_001636057.1) from CHLOROFLEXUS… · 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 A9WHX7
- Elsewhere: RCSB PDB 3KGY · PDBe 3KGY · UniProt A9WHX7
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