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crystal structure of the eucaryotic mono-ADP-ribosyltransferase ART2.2; CRYSTAL FORM A (P21)
Analyse crystal structure of the eucaryotic mono-ADP-ribosyltransferase ART2.2; CRYSTAL… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GXY
- Type
- protein
- Length
- 446 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.71
- Source
- RATTUS NORVEGICUS
- Molecule
- T-cell ecto-ADP-ribosyltransferase 2
- EC
- 2.4.2.31
- UniProt
- P20974
- Pockets
- 5 · best druggability 0.66
Structure
x-ray diffraction · resolution 1.71 · 1 distinct chain · 36% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | T-cell ecto-ADP-ribosyltransferase 2 (EC 2.4.2.31) | protein | 223 | 36% helix, 21% strand | P20974 |
Ligands and binding sites
- GOL · Glycerol · additive · 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 423 | 0.66 | 0.79 | 43 | GOL |
| 2 | 388 | 0.66 | 0.79 | 42 | GOL |
| 3 | 493 | 0.63 | 0.76 | 52 | empty |
| 4 | 57 | 0.31 | 0.76 | 19 | empty |
| 5 | 52 | 0.29 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 304 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1GXY · Crystal structure of the eucaryotic mono-ADP-ribosyltransferase ART2.2; crystal form a… · the same entry in another collection · chain A against A, TM-score 1.00
- P20974 · AlphaFold monomer V2.0 prediction for T-cell ecto-ADP- ribosyltransferase 2 (P20974) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P20974
- Elsewhere: RCSB PDB 1GXY · PDBe 1GXY · UniProt P20974
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