Research workbench
Guanine-specific ADP-ribosyltransferase with NADH and GDP
Analyse Guanine-specific ADP-ribosyltransferase with NADH and GDP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZJ5
- Type
- protein
- Length
- 316 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ADP-ribosyltransferase
- UniProt
- Q9L1E4
- Ligands
- NAI, GDP
- Pockets
- 4 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 21% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ADP-ribosyltransferase | protein | 160 | 21% helix, 24% strand | Q9L1E4 |
| B | ADP-ribosyltransferase | protein | 156 | 21% helix, 25% strand | Q9L1E4 |
Ligands and binding sites
- NAI · 1,4-dihydronicotinamide adenine dinucleotide · ligand · 2 copies · chains A, B
- GDP · Guanosine-5'-diphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 201 | 0.56 | 0.79 | 33 | NAI |
| 2 | 125 | 0.43 | 0.77 | 16 | NAI |
| 3 | 186 | 0.43 | 0.73 | 29 | empty |
| 4 | 54 | 0.33 | 0.78 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 792 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 5ZJ5 · Guanine-specific ADP-ribosyltransferase with NADH and GDP · 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 Q9L1E4
- Elsewhere: RCSB PDB 5ZJ5 · PDBe 5ZJ5 · UniProt Q9L1E4
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