MolNFT v1 · #22921 · protein

Crystal structure of the editing domain of threonyl-tRNA synthetase complexed with serine

1TKE: “Crystal structure of the editing domain of threonyl-tRNA synthetase complexed with serine”. X-ray diffraction, 1 ligand (SER), 1 pocket (best druggability 0.39). MolNFT v1 #22921 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 1TKE
Type: protein
Length: 224 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Threonyl-tRNA synthetase
EC: 6.1.1.3
UniProt: P0A8M3
Ligands: SER
Pockets: 1 · best druggability 0.39

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Threonyl-tRNA synthetase (EC 6.1.1.3)	protein	224	34% helix, 30% strand	P0A8M3

Ligands and binding sites

SER · Serine · ligand · 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	120	0.39	0.75	27	SER

Compared structures

1TKE · Crystal structure of the editing domain of threonyl-tRNA synthetase complexed with serine · the same entry in another collection · chain A against A, TM-score 1.00
P0A8M3 · AlphaFold monomer V2.0 prediction for threonine--tRNA ligase (P0A8M3) · 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 P0A8M3
Elsewhere: RCSB PDB 1TKE · PDBe 1TKE · UniProt P0A8M3

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