MolNFT v1 · #29511 · protein
Adenylation domain of NAD+ dependent DNA ligase from M.TUBERCULOSIS
1ZAU: “Adenylation domain of NAD+ dependent DNA ligase from M.TUBERCULOSIS”. X-ray diffraction, 1 ligand (AMP), 5 pockets (best druggability 0.70). MolNFT v1 #29511 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1ZAU
- Type
- protein
- Length
- 321 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA ligase
- EC
- 6.5.1.2
- UniProt
- P63973
- Ligands
- AMP
- Pockets
- 5 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA ligase (EC 6.5.1.2) | protein | 321 | 32% helix, 16% strand | P63973 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 463 | 0.70 | 0.80 | 63 | AMP |
| 2 | 123 | 0.65 | 0.88 | 33 | empty |
| 3 | 52 | 0.39 | 0.81 | 13 | empty |
| 4 | 95 | 0.35 | 0.74 | 14 | empty |
| 5 | 51 | 0.32 | 0.77 | 13 | empty |
Compared structures
- 1ZAU · Adenylation domain of NAD+ dependent DNA ligase from M.tuberculosis · 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 P63973
- Elsewhere: RCSB PDB 1ZAU · PDBe 1ZAU · UniProt P63973
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