› 5eje

X-ray diffraction
1.9Å resolution

Crystal structure of E. coli Adenylate kinase G56C/T163C double mutant in complex with Ap5a

Released:
DOI: 10.2210/pdb5eje/pdb
PDB entry 5eje coloured by chain, front view.
PDB entry 5eje coloured by chain, side view.
PDB entry 5eje coloured by chain, top view.
Source organism: Escherichia coli O139:H28 str. E24377A
Primary publication:
Structural basis for ligand binding to an enzyme by a conformational selection pathway.
Kovermann M, Grundström C, Sauer-Eriksson AE, Sauer UH, Wolf-Watz M
Proc Natl Acad Sci U S A 114 6298-6303 (2017)
PMID: 28559350

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-159587 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenylate kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 214 amino acids
Theoretical weight: 23.67 KDa
Source organism: Escherichia coli O139:H28 str. E24377A
Expression system: Escherichia coli
UniProt:
  • Canonical: P69441 (Residues: 1-214; Coverage: 100%)
Gene names: JW0463, adk, b0474, dnaW, plsA
Sequence domains:
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

2 bound ligands:
Ligand AP5 2 x AP5
Ligand CO 2 x CO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-2
Unit cell:
a: 73.003Å b: 79.064Å c: 81.834Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.186 0.236
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Role of conformational dynamics in the evolution of novel enzyme function.
Maria-Solano et al. (2018)
4 more

1 mention without citation

Structural basis for ligand binding to an enzyme by a conformational selection pathway.
Kovermann et al. (2017)