› 3h86

X-ray diffraction
2.5Å resolution

Crystal structure of adenylate kinase from Methanococcus maripaludis

Released:
DOI: 10.2210/pdb3h86/pdb
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PDB entry 3h86 coloured by chain, front view.
PDB entry 3h86 coloured by chain, side view.
PDB entry 3h86 coloured by chain, top view.
Source organism: Methanococcus maripaludis
Primary publication:
Crystal structure of a trimeric archaeal adenylate kinase from the mesophile Methanococcus maripaludis with an unusually broad functional range and thermal stability.
Davlieva M, Shamoo Y
Proteins 78 357-64 (2010)
PMID: 19731371

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo trimer (preferred)
homo dodecamer
Assembly name:
PDBe Complex ID:
PDB-CPX-179871 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenylate kinase Chains: A, B, C, G
Molecule details ›
Chains: A, B, C, G
Length: 192 amino acids
Theoretical weight: 21.09 KDa
Source organism: Methanococcus maripaludis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6LYG0 (Residues: 1-192; Coverage: 100%)
Gene names: MMP1031, adkA
Sequence domains: AAA domain
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

1 bound ligand:
Ligand AP5 4 x AP5
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: R3
Unit cell:
a: 102.84Å b: 102.84Å c: 228.72Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.183 0.239
Expression system: Escherichia coli

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Citations

1 review citation

Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.
Bräsen et al. (2014)
7 other articles

1 mention without citation

Insights into the evolution of enzymatic specificity and catalysis: From Asgard archaea to human adenylate kinases.
Verma et al. (2022)

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