MolNFT v1 · #40359 · protein

Crystal structure analysis of S. cerevisiae tryptophanyl tRNA synthetase

2IP1 · Tryptophanyl-tRNA synthetase: “Crystal structure analysis of S. cerevisiae tryptophanyl tRNA synthetase”. X-ray diffraction, 3 pockets (best druggability 0.69). MolNFT v1 #40359 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 2IP1
Type: protein
Length: 371 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tryptophanyl-tRNA synthetase
EC: 6.1.1.2
UniProt: Q12109
Pockets: 3 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tryptophanyl-tRNA synthetase (EC 6.1.1.2)	protein	371	55% helix, 10% strand	Q12109

Ligands and binding sites

PG4 · Tetraethylene glycol · additive · 4 copies · chains A

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

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	596	0.69	0.77	55	PG4
2	61	0.36	0.79	18	empty
3	83	0.34	0.74	18	empty

Compared structures

2IP1 · Crystal Structure Analysis of S. cerevisiae Tryptophanyl tRNA Synthetase · the same entry in another collection · chain A against A, TM-score 1.00
Q12109 · AlphaFold monomer V2.0 prediction for tryptophan--tRNA ligase, cytoplasmic (Q12109) · 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 Q12109
Elsewhere: RCSB PDB 2IP1 · PDBe 2IP1 · UniProt Q12109

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