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Crystal structures of the interacting domains from yeast glutamyl-tRNA synthetase and tRNA aminoacylation and nuclear export cofactor ARC1P reveal a novel function for an old fold

Analyse Crystal structures of the interacting domains from yeast glutamyl-tRNA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2HQT
Type: protein
Length: 2,356 residues
Chains: 20
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P46672

Structure

x-ray diffraction · 14 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	115	—	P46672
B, D, G	—	protein	120	—	P46672
C	—	protein	114	—	P46672
E	—	protein	116	—	P46672
F	—	protein	120	—	P46672
H	—	protein	111	—	P46672
I	—	protein	116	—	P46672
J	—	protein	121	—	P46672
K	—	protein	117	—	P46672
L, O, R	—	protein	119	—	P46672
M, Q	—	protein	117	—	P46672
N, P	—	protein	119	—	P46672
S	—	protein	116	—	P46672
T	—	protein	121	—	P46672

Compared structures

2HQT · Crystal structures of the interacting domains from yeast glutamyl-tRNA synthetase and… · the same entry in another collection · chain K against K, 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 P46672
Elsewhere: RCSB PDB 2HQT · PDBe 2HQT · UniProt P46672

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