› 3l0p

X-ray diffraction
3Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + AMP = 2 ADP
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-111779 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenylate kinase Chain: A
Molecule details ›
Chain: A
Length: 223 amino acids
Theoretical weight: 24.54 KDa
Source organism: Megalodesulfovibrio gigas
Expression system: Escherichia coli
UniProt:
  • Canonical: C7U112 (Residues: 1-223; Coverage: 100%)
Gene names: adk, ak
Sequence domains: Adenylate kinase
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

2 bound ligands:
Ligand FE 1 x FE
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: I222
Unit cell:
a: 38.8Å b: 119.16Å c: 146.71Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.186 0.252
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Normal Mode Analysis as a Routine Part of a Structural Investigation.
Bauer et al. (2019)
4 other articles

1 mention without citation

An Iron Reservoir to the Catalytic Metal: THE RUBREDOXIN IRON IN AN EXTRADIOL DIOXYGENASE.
Liu et al. (2015)