› 4ga6

X-ray diffraction
2.21Å resolution

Crystal structure of AMP phosphorylase C-terminal deletion mutant in complex with substrates

Released:
DOI: 10.2210/pdb4ga6/pdb
PDB entry 4ga6 coloured by chain, front view.
PDB entry 4ga6 coloured by chain, side view.
PDB entry 4ga6 coloured by chain, top view.
Source organism: Thermococcus kodakarensis KOD1
Primary publication:
Structure analysis of archaeal AMP phosphorylase reveals two unique modes of dimerization.
Nishitani Y, Aono R, Nakamura A, Sato T, Atomi H, Imanaka T, Miki K
J Mol Biol 425 2709-21 (2013)
PMID: 23659790

Function and Biology Details

Reaction catalysed: 
AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177259 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:

Ligands and Environments

2 bound ligands:
Ligand AMP 2 x AMP
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P21
Unit cell:
a: 51.177Å b: 87.915Å c: 105.549Å
α: 90° β: 98.77° γ: 90°
R-values:
R R work R free
0.214 0.214 0.226
Expression system: Escherichia coli

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Citations

1 review citation

An overview of 25 years of research on Thermococcus kodakarensis, a genetically versatile model organism for archaeal research.
Rashid et al. (2020)
3 other articles

1 mention without citation

The Prodigal Compound: Return of Ribosyl 1,5-Bisphosphate as an Important Player in Metabolism.
Hove-Jensen et al. (2019)