MolNFT v1 · #141619 · protein
Crystal structure analysis of ttqrs in co-crystallised with ATP
5ZDL · Glutamine--tRNA ligase: “Crystal structure analysis of ttqrs in co-crystallised with ATP”. X-ray diffraction, 2 ligands (ATP, CL), 1 pocket (best druggability 0.69). MolNFT v1 #141619 on GenesisL1: 3D structure, binding sites and…
- PDB
- 5ZDL
- Type
- protein
- Length
- 539 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamine--tRNA ligase
- EC
- 6.1.1.18
- UniProt
- Q5SKU4
- Ligands
- ATP, CL
- Pockets
- 1 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamine--tRNA ligase (EC 6.1.1.18) | protein | 539 | 29% helix, 25% strand | Q5SKU4 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 460 | 0.69 | 0.80 | 39 | ATP |
Compared structures
- 5ZDL · Crystal Structure Analysis of TtQRS in co-crystallised 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 5ZDL · PDBe 5ZDL · UniProt Q5SKU4
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