Research workbench

The crystal structure of the tRNA-specific adenosine deaminase from streptococcus pyogenes

Analyse The crystal structure of the tRNA-specific adenosine deaminase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2NX8
Type: protein
Length: 168 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: TRNA-specific adenosine deaminase
EC: 3.5.4.-
UniProt: Q5XE14
Ligands: ZN, PO4
Pockets: 1 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	TRNA-specific adenosine deaminase (EC 3.5.4.-)	protein	168	45% helix, 19% strand	Q5XE14

Ligands and binding sites

ZN · Zinc ion · metal · chains A
PO4 · Phosphate ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	136	0.47	0.77	28	PO4

Compared structures

2NX8 · The crystal structure of the tRNA-specific adenosine deaminase from Streptococcus pyogenes · the same entry in another collection · chain A against A, TM-score 1.00
Q5XE14 · AlphaFold monomer V2.0 prediction for tRNA-specific adenosine deaminase (Q5XE14) · 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 Q5XE14
Elsewhere: RCSB PDB 2NX8 · PDBe 2NX8 · UniProt Q5XE14

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.