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Structure of P-boronophenylalanyl tRNA synthetase - apo form

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

PDB: 5N5V
Type: protein
Length: 2,465 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q57834
Ligands: CL

Structure

x-ray diffraction · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, D, E, F, G	—	protein	309	—	Q57834
B, H	—	protein	307	—	Q57834
C	—	protein	306	—	Q57834

Ligands and binding sites

CL · Chloride ion · ion · 5 copies · chains A, B, D, E, G

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

Compared structures

5N5V · Structure of p-boronophenylalanyl tRNA synthetase - apo form · the same entry in another collection · chain H against H, TM-score 1.00
Q57834 · AlphaFold monomer V2.0 prediction for tyrosine--tRNA ligase (Q57834) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 Q57834
Elsewhere: RCSB PDB 5N5V · PDBe 5N5V · UniProt Q57834

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