MolNFT v2 · #142493 · protein

Crystal Structure Analysis of TtQRS in complex with ATP

5ZDK · Glutamine--tRNA ligase: “Crystal Structure Analysis of TtQRS in complex with ATP”. X-ray diffraction at 2.45, 4 ligands (ATP, CS, MG), 2 pockets (best druggability 0.73). MolNFT v2 #142493 on GenesisL1: 3D structure, binding sites…

PDB: 5ZDK
Type: protein
Length: 543 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.45
Source: Thermus thermophilus HB8
Molecule: Glutamine--tRNA ligase
EC: 6.1.1.18
UniProt: Q5SKU4
Ligands: ATP, CS, MG, CL
Pockets: 2 · best druggability 0.73

Structure

x-ray diffraction · resolution 2.45 · 1 distinct chain · 28% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutamine--tRNA ligase (EC 6.1.1.18)	protein	543	28% helix, 25% strand	Q5SKU4

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · chains A
CS · Cesium ion · metal · 2 copies · chains A
MG · Magnesium ion · metal · 2 copies · chains A
CL · Chloride 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	61	0.73	0.98	16	empty
2	412	0.69	0.81	42	ATP, CS, MG

Compared structures

5ZDK · Crystal structure analysis of ttqrs in complex with ATP · 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 Q5SKU4
Elsewhere: RCSB PDB 5ZDK · PDBe 5ZDK · UniProt Q5SKU4

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