› 2ofx

X-ray diffraction
1.9Å resolution

crystal structure of the APSK domain of human PAPSS1 in complex with ADPMg and PAPS

Released:
DOI: 10.2210/pdb2ofx/pdb
PDB entry 2ofx coloured by chain, front view.
PDB entry 2ofx coloured by chain, side view.
PDB entry 2ofx coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Elucidation of the active conformation of the APS-kinase domain of human PAPS synthetase 1.
Sekulic N, Dietrich K, Paarmann I, Ort S, Konrad M, Lavie A
J Mol Biol 367 488-500 (2007)
PMID: 17276460

Function and Biology Details

Reactions catalysed: 
ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate
ATP + sulfate = diphosphate + adenylyl sulfate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128876 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 207 amino acids
Theoretical weight: 22.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O43252 (Residues: 25-227; Coverage: 33%)
Gene names: ATPSK1, PAPSS, PAPSS1
Sequence domains: Adenylylsulphate kinase
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

4 bound ligands:
Ligand MG 2 x MG
Ligand PO4 4 x PO4
Ligand PPS 2 x PPS
Ligand ADP 2 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P21
Unit cell:
a: 51.4Å b: 63.32Å c: 61.69Å
α: 90° β: 114.38° γ: 90°
R-values:
R R work R free
0.192 0.187 0.236
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Adenosine-5'-phosphosulfate--a multifaceted modulator of bifunctional 3'-phospho-adenosine-5'-phosphosulfate synthases and related enzymes.
Mueller et al. (2013)
1 more

6 mentions without citation

The SARS coronavirus nucleocapsid protein--forms and functions.
Chang et al. (2014)
5 more