MolNFT v1 · #8343 · protein
Crystal structure of the eucaryotic mono-ADP-ribosyltransferase ART2.2; crystal form C (P3121)
1GY0 · T-cell ecto-ADP-ribosyltransferase 2: “Crystal structure of the eucaryotic mono-ADP-ribosyltransferase ART2.2; crystal form C (P3121)”. X-ray diffraction, 2 pockets (best druggability 0.64). MolNFT v1 #8343 on GenesisL1: 3D…
- PDB
- 1GY0
- Type
- protein
- Length
- 223 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- T-cell ecto-ADP-ribosyltransferase 2
- EC
- 2.4.2.31
- UniProt
- P20974
- Pockets
- 2 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | T-cell ecto-ADP-ribosyltransferase 2 (EC 2.4.2.31) | protein | 223 | 35% helix, 21% strand | P20974 |
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 | 375 | 0.64 | 0.79 | 43 | empty |
| 2 | 86 | 0.38 | 0.77 | 17 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1GY0 · crystal structure of the eucaryotic mono-ADP-ribosyltransferase ART2.2; CRYSTAL FORM C… · 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 0.98
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 1GY0 · PDBe 1GY0 · UniProt P20974
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.