› 1e4v

X-ray diffraction
1.85Å resolution

Mutant G10V of adenylate kinase from E. coli, modified in the Gly-loop

Released:
DOI: 10.2210/pdb1e4v/pdb
PDB entry 1e4v coloured by chain, front view.
PDB entry 1e4v coloured by chain, side view.
PDB entry 1e4v coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structures of two mutants of adenylate kinase from Escherichia coli that modify the Gly-loop.
Müller CW, Schulz GE
Proteins 15 42-9 (1993)
PMID: 8451239

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenylate kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 214 amino acids
Theoretical weight: 23.66 KDa
Source organism: Escherichia coli
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

1 bound ligand:
Ligand AP5 2 x AP5
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Unit cell:
a: 73.2Å b: 79.8Å c: 85Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.196 not available
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Protein conformational substates from X-ray crystallography.
Rejto et al. (1996)
17 other articles

8 mentions without citation

Conformational heterogeneity within the LID domain mediates substrate binding to Escherichia coli adenylate kinase: function follows fluctuations.
Schrank et al. (2013)
7 more