Research workbench
The crystal structure of C3STAU2 from S. aureus in with NAD
Analyse The crystal structure of C3STAU2 from S. aureus in with NAD in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OJZ
- Type
- protein
- Length
- 212 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ADP-ribosyltransferase
- UniProt
- Q9ADS9
- Ligands
- NAD
- Pockets
- 2 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ADP-ribosyltransferase | protein | 212 | 36% helix, 24% strand | Q9ADS9 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 177 | 0.52 | 0.79 | 22 | NAD |
| 2 | 52 | 0.34 | 0.78 | 13 | empty |
Compared structures
- 1OJZ · The crystal structure of C3stau2 from S. aureus with NAD · 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 Q9ADS9
- Elsewhere: RCSB PDB 1OJZ · PDBe 1OJZ · UniProt Q9ADS9
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