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Crystal structure of the apo form of the glutaminyl-tRNA synthetase catalytic domain from toxoplasma gondii.

Analyse Crystal structure of the apo form of the glutaminyl-tRNA synthetase catalytic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4P2B
Type: protein
Length: 507 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutamine aminoacyl-tRNA synthetase
UniProt: D3XAP9
Ligands: SO4
Pockets: 2 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutamine aminoacyl-tRNA synthetase	protein	507	30% helix, 24% strand	D3XAP9

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	112	0.68	0.90	26	empty
2	537	0.67	0.78	64	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

4P2B · Crystal structure of the apo form of the glutaminyl-tRNA synthetase catalytic domain from… · the same entry in another collection · chain A against A, TM-score 1.00

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 D3XAP9
Elsewhere: RCSB PDB 4P2B · PDBe 4P2B · UniProt D3XAP9

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