Research workbench
Crystal structure of dihydrofolate reductase from mycobacterium kansasii in complex with NADP and inhibitor P218
Analyse Crystal structure of dihydrofolate reductase from mycobacterium kansasii in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7K62
- Type
- protein
- Length
- 330 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydrofolate reductase
- EC
- 1.5.1.3
- UniProt
- A0A1V3XYG5
- Ligands
- NAP, MMV
- Pockets
- 2 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 21% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Dihydrofolate reductase (EC 1.5.1.3) | protein | 165 | 21% helix, 32% strand | A0A1V3XYG5 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- MMV · 3-(2-{3-[(2,4-diamino-6-ethylpyrimidin-5-yl) oxy]propoxy}phenyl)propanoic acid · ligand · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 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 | 865 | 0.73 | 0.78 | 87 | NAP, MMV, EDO |
| 2 | 499 | 0.71 | 0.81 | 50 | NAP, MMV, EDO |
Interfaces
1 interface between chains.
- A–B · 359 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 7K62 · Crystal Structure of Dihydrofolate reductase from Mycobacterium kansasii in complex with… · 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 A0A1V3XYG5
- Elsewhere: RCSB PDB 7K62 · PDBe 7K62 · UniProt A0A1V3XYG5
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