Research workbench
Crystal structure of a NAD kinase from archaeoglobus fulgidus bound by NADP
Analyse Crystal structure of a NAD kinase from archaeoglobus fulgidus bound by NADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Z0U
- Type
- protein
- Length
- 498 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable inorganic POLYPHOSPHATE/ATP-NAD kinase
- EC
- 2.7.1.23
- UniProt
- O30297
- Ligands
- NAP, SO4
- Pockets
- 4 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 21% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Probable inorganic POLYPHOSPHATE/ATP-NAD kinase (EC 2.7.1.23) | protein | 249 | 21% helix, 41% strand | O30297 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 3 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 | 166 | 0.56 | 0.81 | 37 | NAP |
| 2 | 177 | 0.56 | 0.80 | 29 | NAP |
| 3 | 116 | 0.46 | 0.79 | 21 | empty |
| 4 | 126 | 0.46 | 0.78 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 1259 Ų buried · 21 hydrogen bonds · protein-protein
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 O30297
- Elsewhere: RCSB PDB 1Z0U · PDBe 1Z0U · UniProt O30297
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