› 1m7g

X-ray diffraction
1.43Å resolution

Crystal structure of APS kinase from Penicillium Chrysogenum: Ternary structure with ADP and APS

Released:
DOI: 10.2210/pdb1m7g/pdb
PDB entry 1m7g coloured by chain, front view.
PDB entry 1m7g coloured by chain, side view.
PDB entry 1m7g coloured by chain, top view.
Source organism: Penicillium chrysogenum
Primary publication:
Ligand-induced structural changes in adenosine 5'-phosphosulfate kinase from Penicillium chrysogenum.
Lansdon EB, Segel IH, Fisher AJ
Biochemistry 41 13672-80 (2002)
PMID: 12427029

Function and Biology Details

Reaction catalysed: 
ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-171380 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenylyl-sulfate kinase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 211 amino acids
Theoretical weight: 23.8 KDa
Source organism: Penicillium chrysogenum
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q12657 (Residues: 1-211; Coverage: 100%)
Sequence domains: Adenylylsulphate kinase
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

5 bound ligands:
Ligand SO4 6 x SO4
Ligand AV2 2 x AV2
Ligand ADX 4 x ADX
Ligand ADP 2 x ADP
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P212121
Unit cell:
a: 81.52Å b: 84.32Å c: 137.26Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.18 0.205
Expression system: Escherichia coli BL21

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Citations

2 review citations

The power of vanadate in crystallographic investigations of phosphoryl transfer enzymes.
Davies et al. (2004)
1 more

9 mentions without citation

Crystal structure of Escherichia coli cytidine triphosphate synthetase, a nucleotide-regulated glutamine amidotransferase/ATP-dependent amidoligase fusion protein and homologue of anticancer and antiparasitic drug targets.
Endrizzi et al. (2004)
8 more