Research workbench
X-ray crystal structure of a nicotinate nucleotide adenylyltransferase from burkholderia thailandensis bound to NAD
Analyse X-ray crystal structure of a nicotinate nucleotide adenylyltransferase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4WSO
- Type
- protein
- Length
- 454 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable nicotinate-nucleotide adenylyltransferase
- EC
- 2.7.7.18
- UniProt
- Q2SZT3
- Ligands
- NAD, PO4
- Pockets
- 4 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Probable nicotinate-nucleotide adenylyltransferase (EC 2.7.7.18) | protein | 227 | 41% helix, 15% strand | Q2SZT3 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · 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 | 435 | 0.79 | 0.87 | 55 | NAD, PO4 |
| 2 | 505 | 0.79 | 0.86 | 63 | NAD, PO4 |
| 3 | 97 | 0.40 | 0.77 | 20 | empty |
| 4 | 64 | 0.36 | 0.78 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 387 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 4WSO · X-ray crystal structure of a nicotinate nucleotide adenylyltransferase from Burkholderia… · 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 Q2SZT3
- Elsewhere: RCSB PDB 4WSO · PDBe 4WSO · UniProt Q2SZT3
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