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Crystal structure of the editing domain of threonyl-tRNA synthetase complexed with seryl-3'-aminoadenosine

Analyse Crystal structure of the editing domain of threonyl-tRNA synthetase complexed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1TKY
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: A3S
Pockets: 1 · best druggability 0.38

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

A3S · Serine-3'-aminoadenosine · 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	97	0.38	0.75	19	A3S

Compared structures

1TKY · Crystal structure of the editing domain of threonyl-tRNA synthetase complexed with… · 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 1TKY · PDBe 1TKY · UniProt P0A8M3

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