Research workbench
Guanine-specific ADP-ribosyltransferase
Analyse Guanine-specific ADP-ribosyltransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZJ4
- Type
- protein
- Length
- 640 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ADP-ribosyltransferase
- UniProt
- Q9L1E4
- Pockets
- 11 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 22% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | ADP-ribosyltransferase | protein | 160 | 22% helix, 24% strand | Q9L1E4 |
Ligands and binding sites
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 257 | 0.61 | 0.80 | 32 | MPD |
| 2 | 205 | 0.59 | 0.81 | 26 | empty |
| 3 | 222 | 0.58 | 0.80 | 30 | empty |
| 4 | 213 | 0.56 | 0.79 | 27 | empty |
| 5 | 229 | 0.51 | 0.76 | 33 | empty |
Interfaces
5 interfaces between chains.
- A–C · 834 Ų buried · 17 hydrogen bonds · protein-protein
- B–D · 789 Ų buried · 15 hydrogen bonds · protein-protein
- A–B · 408 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 145 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 105 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 5ZJ4 · Guanine-specific ADP-ribosyltransferase · 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 5ZJ4 · PDBe 5ZJ4 · UniProt Q9L1E4
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