MolNFT v1 · #134857 · protein

Crystal structure of a human tyrosyl-tRNA synthetase mutant

5THH · Tyrosine--tRNA ligase, cytoplasmic: “Crystal structure of a human tyrosyl-tRNA synthetase mutant”. X-ray diffraction, 1 ligand (TYR), 3 pockets (best druggability 0.69). MolNFT v1 #134857 on GenesisL1: 3D structure, binding sites…

PDB: 5THH
Type: protein
Length: 329 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tyrosine--tRNA ligase, cytoplasmic
EC: 6.1.1.1
UniProt: P54577
Ligands: TYR
Pockets: 3 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine--tRNA ligase, cytoplasmic (EC 6.1.1.1)	protein	329	54% helix, 12% strand	P54577

Ligands and binding sites

TYR · Tyrosine · ligand · 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	468	0.69	0.80	46	TYR
2	57	0.47	0.84	14	empty
3	92	0.37	0.75	12	empty

Compared structures

5THH · Crystal structure of a human tyrosyl-tRNA synthetase mutant · the same entry in another collection · chain A against A, TM-score 1.00
P54577 · AlphaFold monomer V2.0 prediction for tyrosine--tRNA ligase, cytoplasmic (P54577) · 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 P54577
Elsewhere: RCSB PDB 5THH · PDBe 5THH · UniProt P54577

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