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Quaternary complex of mutant T252A of E. COLI leucyl-tRNA synthetase with TRNA(LEU), leucyl-adenylate analogue, and post-transfer editing analogue of norvaline in the aminoacylation conformation

Analyse Quaternary complex of mutant T252A of E. COLI leucyl-tRNA synthetase with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5ON2
Type: protein + RNA
Length: 1,889 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P07813
Ligands: LSS, ZN, MG

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	863	—	P07813
B	—	rna	85	—	—
D	—	protein	861	—	P07813
E	—	rna	80	—	—

Ligands and binding sites

LSS · 5'-O-(L-leucylsulfamoyl)adenosine · ligand · 2 copies · chains A, B, D, E
ZN · Zinc ion · metal · 2 copies · chains A, D
MG · Magnesium ion · metal · 2 copies · chains B, E

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

Compared structures

5ON2 · Quaternary complex of mutant T252A of E. coli leucyl-tRNA synthetase with tRNA(leu)… · the same entry in another collection · chain B against B, TM-score 1.00
P07813 · AlphaFold monomer V2.0 prediction for leucine--tRNA ligase (P07813) · a predicted model of the same protein · chain D against A, TM-score 0.90

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P07813
Elsewhere: RCSB PDB 5ON2 · PDBe 5ON2 · UniProt P07813

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