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Crystal structure of the N-terminal anticodon-binding domain of non- discriminating aspartyl-tRNA synthetase from helicobacter pylori

Analyse Crystal structure of the N-terminal anticodon-binding domain of non… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5GRO
Type: protein
Length: 206 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aspartate--TRNA(ASP/ASN) ligase
EC: 6.1.1.23
UniProt: P56459
Ligands: BUA

Structure

x-ray diffraction · 1 distinct chain · 10% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Aspartate--TRNA(ASP/ASN) ligase (EC 6.1.1.23)	protein	103	10% helix, 49% strand	P56459

Ligands and binding sites

BUA · butanoic acid · ligand · chains B
GOL · Glycerol · additive · 2 copies · chains A, B
IMD · Imidazole · additive · chains B

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

Interfaces

1 interface between chains.

A–B · 1008 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

5GRO · Crystal structure of the N-terminal anticodon-binding domain of non-discriminating… · the same entry in another collection · chain A against A, TM-score 1.00
P56459 · AlphaFold monomer V2.0 prediction for aspartate--TRNA(ASP/ASN) ligase (P56459) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P56459
Elsewhere: RCSB PDB 5GRO · PDBe 5GRO · UniProt P56459

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