MolNFT v1 · #23369 · protein

Structural analysis of a series of mutants of tyrosyl-tRNA synthetase: enhancement of catalysis by hydrophobic interactions

1TYA: “Structural analysis of a series of mutants of tyrosyl-tRNA synthetase: enhancement of catalysis by…”. X-ray diffraction, 1 ligand (TYR), 3 pockets (best druggability 0.69). MolNFT v1 #23369 on GenesisL1: 3D structure, binding sites…

PDB: 1TYA
Type: protein
Length: 317 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tyrosyl-tRNA synthetase
EC: 6.1.1.1
UniProt: P00952
Ligands: TYR
Pockets: 3 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E	Tyrosyl-tRNA synthetase (EC 6.1.1.1)	protein	317	54% helix, 10% strand	P00952

Ligands and binding sites

TYR · Tyrosine · ligand · chains E

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	432	0.69	0.81	41	TYR
2	141	0.42	0.74	22	empty
3	58	0.33	0.77	20	empty

Compared structures

1TYA · Structural analysis of a series of mutants of tyrosyl-tRNA synthetase: enhancement of… · the same entry in another collection · chain E against E, TM-score 1.00
P00952 · AlphaFold monomer V2.0 prediction for tyrosine--tRNA ligase (P00952) · a predicted model of the same protein · chain E 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 P00952
Elsewhere: RCSB PDB 1TYA · PDBe 1TYA · UniProt P00952

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