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Isoleucyl-tRNA synthetase editing domain complexed with the post-transfer editing substrate analogue, val-2AA

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

PDB: 1WNZ
Type: protein
Length: 180 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Isoleucyl-tRNA synthetase
EC: 6.1.1.5
UniProt: P56690
Ligands: 2VA
Pockets: 1 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Isoleucyl-tRNA synthetase (EC 6.1.1.5)	protein	180	24% helix, 31% strand	P56690

Ligands and binding sites

2VA · 2'-(L-valyl)amino-2'-deoxyadenosine · 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	110	0.40	0.76	19	2VA

Compared structures

1WNZ · Isoleucyl-tRNA synthetase editing domain complexed with the post-transfer editing… · the same entry in another collection · chain A against A, TM-score 1.00
P56690 · AlphaFold monomer V2.0 prediction for isoleucine--tRNA ligase (P56690) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P56690
Elsewhere: RCSB PDB 1WNZ · PDBe 1WNZ · UniProt P56690

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