› 2a3l

X-ray diffraction
3.34Å resolution

X-Ray Structure of Adenosine 5'-Monophosphate Deaminase from Arabidopsis Thaliana in Complex with Coformycin 5'-Phosphate

Released:
DOI: 10.2210/pdb2a3l/pdb
PDB entry 2a3l coloured by chain, front view.
PDB entry 2a3l coloured by chain, side view.
PDB entry 2a3l coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Membrane association, mechanism of action, and structure of Arabidopsis embryonic factor 1 (FAC1).
Han BW, Bingman CA, Mahnke DK, Bannen RM, Bednarek SY, Sabina RL, Phillips GN
J Biol Chem 281 14939-47 (2006)
PMID: 16543243

Function and Biology Details

Reaction catalysed: 
AMP + H(2)O = IMP + NH(3)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-131322 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
AMP deaminase Chain: A
Molecule details ›
Chain: A
Length: 701 amino acids
Theoretical weight: 80.41 KDa
Source organism: Arabidopsis thaliana
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: O80452 (Residues: 139-839; Coverage: 84%)
Gene names: AMPD, At2g38280, F16M14.21, FAC1
Sequence domains: AMP deaminase
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand ZN 1 x ZN
Ligand PO4 1 x PO4
Ligand CF5 1 x CF5
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P6222
Unit cell:
a: 131.325Å b: 131.325Å c: 208.254Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.237 0.237 0.323
Expression system: Spodoptera frugiperda

Quick links

Citations

3 review citations

Normal Mode Analysis as a Routine Part of a Structural Investigation.
Bauer et al. (2019)
2 more

5 mentions without citation

Ligands in PSI structures.
Kumar et al. (2010)
4 more