Research workbench
Deoxyhypusine synthase holoenzyme in its low ionic strength, high pH crystal form
Analyse Deoxyhypusine synthase holoenzyme in its low ionic strength, high pH crystal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ROZ
- Type
- protein
- Length
- 657 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Deoxyhypusine synthase
- EC
- 2.5.1.46
- UniProt
- P49366
- Ligands
- NAD
- Pockets
- 5 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 52% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Deoxyhypusine synthase (EC 2.5.1.46) | protein | 336 | 51% helix, 12% strand | P49366 |
| B | Deoxyhypusine synthase (EC 2.5.1.46) | protein | 321 | 52% helix, 12% strand | P49366 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B
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 | 455 | 0.63 | 0.76 | 59 | empty |
| 2 | 217 | 0.59 | 0.80 | 30 | empty |
| 3 | 156 | 0.49 | 0.78 | 18 | empty |
| 4 | 84 | 0.32 | 0.73 | 15 | empty |
| 5 | 66 | 0.29 | 0.73 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 2560 Ų buried · 39 hydrogen bonds · protein-protein
Compared structures
- 1ROZ · Deoxyhypusine synthase holoenzyme in its low ionic strength, high pH crystal form · the same entry in another collection · chain A against A, TM-score 1.00
- P49366 · AlphaFold monomer V2.0 prediction for deoxyhypusine synthase (P49366) · a predicted model of the same protein · chain B 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 P49366
- Elsewhere: RCSB PDB 1ROZ · PDBe 1ROZ · UniProt P49366
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