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Structural basis for inhbition of NAD-dependent ligase
Analyse Structural basis for inhbition of NAD-dependent ligase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BA9
- Type
- protein
- Length
- 313 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA ligase
- EC
- 6.5.1.2
- UniProt
- Q837V6
- Ligands
- NMN, 3B9, SO4
- Pockets
- 4 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA ligase (EC 6.5.1.2) | protein | 313 | 42% helix, 23% strand | Q837V6 |
Ligands and binding sites
- NMN · Beta-nicotinamide ribose monophosphate · ligand · chains A
- 3B9 · N-[2-(2,4-diaminopyrido[2,3-d]pyrimidin-7-yl)-2-methylpropyl]-4-phenoxybenzamide · ligand · chains A
- SO4 · Sulfate ion · ion · 4 copies · chains A
- GOL · Glycerol · additive · 3 copies · chains A
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 | 413 | 0.71 | 0.82 | 46 | SO4, 3B9, GOL |
| 2 | 185 | 0.55 | 0.80 | 26 | empty |
| 3 | 71 | 0.36 | 0.77 | 23 | empty |
| 4 | 57 | 0.35 | 0.78 | 14 | empty |
Compared structures
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 Q837V6
- Elsewhere: RCSB PDB 3BA9 · PDBe 3BA9 · UniProt Q837V6
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