› 1fl0

X-ray diffraction
1.5Å resolution

CRYSTAL STRUCTURE OF THE EMAP2/RNA-BINDING DOMAIN OF THE P43 PROTEIN FROM HUMAN AMINOACYL-TRNA SYNTHETASE COMPLEX

Released:
DOI: 10.2210/pdb1fl0/pdb
PDB entry 1fl0 coloured by chain, front view.
PDB entry 1fl0 coloured by chain, side view.
PDB entry 1fl0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the EMAPII domain of human aminoacyl-tRNA synthetase complex reveals evolutionary dimer mimicry.
Renault L, Kerjan P, Pasqualato S, Ménétrey J, Robinson JC, Kawaguchi S, Vassylyev DG, Yokoyama S, Mirande M, Cherfils J
EMBO J 20 570-8 (2001)
PMID: 11157763

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171431 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endothelial monocyte-activating polypeptide 2 Chain: A
Molecule details ›
Chain: A
Length: 171 amino acids
Theoretical weight: 19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q12904 (Residues: 150-312; Coverage: 52%)
Gene names: AIMP1, EMAP2, SCYE1
Sequence domains: Putative tRNA binding domain
Structure domains: Nucleic acid-binding proteins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LURE BEAMLINE DW32
Spacegroup: P21
Unit cell:
a: 35.954Å b: 59.683Å c: 37.85Å
α: 90° β: 114.83° γ: 90°
R-values:
R R work R free
0.221 0.221 0.224
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Evolution of protein structures and functions.
Kinch et al. (2002)
7 more

8 mentions without citation

Functional expansion of human tRNA synthetases achieved by structural inventions.
Guo et al. (2010)
7 more